PDB ID: pdb_00008sqr
- Crystal Structure of Bacterioferritin (Bfr) from Brucella abortus (iron bound, F16L mutant)
- Experimental method: X-RAY DIFFRACTION
- Resolution: 1.65 Å
- Deposition date: 2023-05-04
Number of assemblies: 1
| Structural data | modeled |
|---|---|
| Oligomeric count | 24 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
B (MG  MG
), B-1 (MGMG
), B-10 (MGMG
), B-11 (MGMG
), B-12 (MGMG
), B-13 (MGMG
), B-14 (MGMG
), B-15 (MGMG
), B-16 (MGMG
), B-17 (MGMG
), B-18 (MGMG
), B-19 (MGMG
), B-2 (MGMG
), B-20 (MGMG
), B-21 (MGMG
), B-22 (MGMG
), B-23 (MGMG
), B-3 (MGMG
), B-4 (MGMG
), B-5 (MGMG
), B-6 (MGMG
), B-7 (MGMG
), B-8 (MGMG
), B-9 (MGMG
), C (MGMG
), C-1 (MGMG
), C-10 (MGMG
), C-11 (MGMG
), C-12 (MGMG
), C-13 (MGMG
), C-14 (MGMG
), C-15 (MGMG
), C-16 (MGMG
), C-17 (MGMG
), C-18 (MGMG
), C-19 (MGMG
), C-2 (MGMG
), C-20 (MGMG
), C-21 (MGMG
), C-22 (MGMG
), C-23 (MGMG
), C-3 (MGMG
), C-4 (MGMG
), C-5 (MGMG
), C-6 (MGMG
), C-7 (MGMG
), C-8 (MGMG
), C-9 (MGMG
), D (SO4 SO4
), D-1 (SO4SO4
), D-10 (SO4SO4
), D-11 (SO4SO4
), D-12 (SO4SO4
), D-13 (SO4SO4
), D-14 (SO4SO4
), D-15 (SO4SO4
), D-16 (SO4SO4
), D-17 (SO4SO4
), D-18 (SO4SO4
), D-19 (SO4SO4
), D-2 (SO4SO4
), D-20 (SO4SO4
), D-21 (SO4SO4
), D-22 (SO4SO4
), D-23 (SO4SO4
), D-3 (SO4SO4
), D-4 (SO4SO4
), D-5 (SO4SO4
), D-6 (SO4SO4
), D-7 (SO4SO4
), D-8 (SO4SO4
), D-9 (SO4SO4
), E (SO4SO4
), E-1 (SO4SO4
), E-10 (SO4SO4
), E-11 (SO4SO4
), E-12 (SO4SO4
), E-13 (SO4SO4
), E-14 (SO4SO4
), E-15 (SO4SO4
), E-16 (SO4SO4
), E-17 (SO4SO4
), E-18 (SO4SO4
), E-19 (SO4SO4
), E-2 (SO4SO4
), E-20 (SO4SO4
), E-21 (SO4SO4
), E-22 (SO4SO4
), E-23 (SO4SO4
), E-3 (SO4SO4
), E-4 (SO4SO4
), E-5 (SO4SO4
), E-6 (SO4SO4
), E-7 (SO4SO4
), E-8 (SO4SO4
), E-9 (SO4SO4
), F (CL CL
), F-1 (CLCL
), F-10 (CLCL
), F-11 (CLCL
), F-12 (CLCL
), F-13 (CLCL
), F-14 (CLCL
), F-15 (CLCL
), F-16 (CLCL
), F-17 (CLCL
), F-18 (CLCL
), F-19 (CLCL
), F-2 (CLCL
), F-20 (CLCL
), F-21 (CLCL
), F-22 (CLCL
), F-23 (CLCL
), F-3 (CLCL
), F-4 (CLCL
), F-5 (CLCL
), F-6 (CLCL
), F-7 (CLCL
), F-8 (CLCL
), F-9 (CLCL
), G (CLCL
), G-1 (CLCL
), G-10 (CLCL
), G-11 (CLCL
), G-12 (CLCL
), G-13 (CLCL
), G-14 (CLCL
), G-15 (CLCL
), G-16 (CLCL
), G-17 (CLCL
), G-18 (CLCL
), G-19 (CLCL
), G-2 (CLCL
), G-20 (CLCL
), G-21 (CLCL
), G-22 (CLCL
), G-23 (CLCL
), G-3 (CLCL
), G-4 (CLCL
), G-5 (CLCL
), G-6 (CLCL
), G-7 (CLCL
), G-8 (CLCL
), G-9 (CLCL
), H (CLCL
), H-1 (CLCL
), H-10 (CLCL
), H-11 (CLCL
), H-12 (CLCL
), H-13 (CLCL
), H-14 (CLCL
), H-15 (CLCL
), H-16 (CLCL
), H-17 (CLCL
), H-18 (CLCL
), H-19 (CLCL
), H-2 (CLCL
), H-20 (CLCL
), H-21 (CLCL
), H-22 (CLCL
), H-23 (CLCL
), H-3 (CLCL
), H-4 (CLCL
), H-5 (CLCL
), H-6 (CLCL
), H-7 (CLCL
), H-8 (CLCL
), H-9 (CLCL
), I (FE2 FE2
), I-1 (FE2FE2
), I-10 (FE2FE2
), I-11 (FE2FE2
), I-12 (FE2FE2
), I-13 (FE2FE2
), I-14 (FE2FE2
), I-15 (FE2FE2
), I-16 (FE2FE2
), I-17 (FE2FE2
), I-18 (FE2FE2
), I-19 (FE2FE2
), I-2 (FE2FE2
), I-20 (FE2FE2
), I-21 (FE2FE2
), I-22 (FE2FE2
), I-23 (FE2FE2
), I-3 (FE2FE2
), I-4 (FE2FE2
), I-5 (FE2FE2
), I-6 (FE2FE2
), I-7 (FE2FE2
), I-8 (FE2FE2
), I-9 (FE2FE2
), J (FE2FE2
), J-1 (FE2FE2
), J-10 (FE2FE2
), J-11 (FE2FE2
), J-12 (FE2FE2
), J-13 (FE2FE2
), J-14 (FE2FE2
), J-15 (FE2FE2
), J-16 (FE2FE2
), J-17 (FE2FE2
), J-18 (FE2FE2
), J-19 (FE2FE2
), J-2 (FE2FE2
), J-20 (FE2FE2
), J-21 (FE2FE2
), J-22 (FE2FE2
), J-23 (FE2FE2
), J-3 (FE2FE2
), J-4 (FE2FE2
), J-5 (FE2FE2
), J-6 (FE2FE2
), J-7 (FE2FE2
), J-8 (FE2FE2
), J-9 (FE2FE2
), K (FE2FE2
), K-1 (FE2FE2
), K-10 (FE2FE2
), K-11 (FE2FE2
), K-12 (FE2FE2
), K-13 (FE2FE2
), K-14 (FE2FE2
), K-15 (FE2FE2
), K-16 (FE2FE2
), K-17 (FE2FE2
), K-18 (FE2FE2
), K-19 (FE2FE2
), K-2 (FE2FE2
), K-20 (FE2FE2
), K-21 (FE2FE2
), K-22 (FE2FE2
), K-23 (FE2FE2
), K-3 (FE2FE2
), K-4 (FE2FE2
), K-5 (FE2FE2
), K-6 (FE2FE2
), K-7 (FE2FE2
), K-8 (FE2FE2
), K-9 (FE2FE2
), L (FE2FE2
), L-1 (FE2FE2
), L-10 (FE2FE2
), L-11 (FE2FE2
), L-12 (FE2FE2
), L-13 (FE2FE2
), L-14 (FE2FE2
), L-15 (FE2FE2
), L-16 (FE2FE2
), L-17 (FE2FE2
), L-18 (FE2FE2
), L-19 (FE2FE2
), L-2 (FE2FE2
), L-20 (FE2FE2
), L-21 (FE2FE2
), L-22 (FE2FE2
), L-23 (FE2FE2
), L-3 (FE2FE2
), L-4 (FE2FE2
), L-5 (FE2FE2
), L-6 (FE2FE2
), L-7 (FE2FE2
), L-8 (FE2FE2
), L-9 (FE2FE2
), M (FE2FE2
), M-1 (FE2FE2
), M-10 (FE2FE2
), M-11 (FE2FE2
), M-12 (FE2FE2
), M-13 (FE2FE2
), M-14 (FE2FE2
), M-15 (FE2FE2
), M-16 (FE2FE2
), M-17 (FE2FE2
), M-18 (FE2FE2
), M-19 (FE2FE2
), M-2 (FE2FE2
), M-20 (FE2FE2
), M-21 (FE2FE2
), M-22 (FE2FE2
), M-23 (FE2FE2
), M-3 (FE2FE2
), M-4 (FE2FE2
), M-5 (FE2FE2
), M-6 (FE2FE2
), M-7 (FE2FE2
), M-8 (FE2FE2
), M-9 (FE2FE2
), N (ACT ACT
), N-1 (ACTACT
), N-10 (ACTACT
), N-11 (ACTACT
), N-12 (ACTACT
), N-13 (ACTACT
), N-14 (ACTACT
), N-15 (ACTACT
), N-16 (ACTACT
), N-17 (ACTACT
), N-18 (ACTACT
), N-19 (ACTACT
), N-2 (ACTACT
), N-20 (ACTACT
), N-21 (ACTACT
), N-22 (ACTACT
), N-23 (ACTACT
), N-3 (ACTACT
), N-4 (ACTACT
), N-5 (ACTACT
), N-6 (ACTACT
), N-7 (ACTACT
), N-8 (ACTACT
), N-9 (ACTACT
), P (MPD MPD
), P-1 (MPDMPD
), P-10 (MPDMPD
), P-11 (MPDMPD
), P-12 (MPDMPD
), P-13 (MPDMPD
), P-14 (MPDMPD
), P-15 (MPDMPD
), P-16 (MPDMPD
), P-17 (MPDMPD
), P-18 (MPDMPD
), P-19 (MPDMPD
), P-2 (MPDMPD
), P-20 (MPDMPD
), P-21 (MPDMPD
), P-22 (MPDMPD
), P-23 (MPDMPD
), P-3 (MPDMPD
), P-4 (MPDMPD
), P-5 (MPDMPD
), P-6 (MPDMPD
), P-7 (MPDMPD
), P-8 (MPDMPD
), P-9 (MPDMPD
)
|
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-1 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-10 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-11 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-1 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-3 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-2 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-10 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-11 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-9 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-8 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-2 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-7 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-6 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-4 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-5 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-3 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-4 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-5 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-6 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-7 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-8 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-159 (1-161) |
| Mutations (UniProt numbering) | |
| Missing residues | 77LEU-77LEU |
| Structural gaps | Exists |
| Uniprot ID | Q2YKI4 ￫UniprotKB |
| label_asym_ids of heme | O-9 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |