Danish
PDB ID:  pdb_00008sqp
  • Crystal Structure of Bacterioferritin (Bfr) from Brucella abortus (Apo, F16L mutant)
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • Deposition date: 2023-05-04
Number of assemblies:  1
Assembly ID:  1  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 24
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others B (CLStructure of CLCL ), B-1 (CLStructure of CLCL ), B-10 (CLStructure of CLCL ), B-11 (CLStructure of CLCL ), B-12 (CLStructure of CLCL ), B-13 (CLStructure of CLCL ), B-14 (CLStructure of CLCL ), B-15 (CLStructure of CLCL ), B-16 (CLStructure of CLCL ), B-17 (CLStructure of CLCL ), B-18 (CLStructure of CLCL ), B-19 (CLStructure of CLCL ), B-2 (CLStructure of CLCL ), B-20 (CLStructure of CLCL ), B-21 (CLStructure of CLCL ), B-22 (CLStructure of CLCL ), B-23 (CLStructure of CLCL ), B-3 (CLStructure of CLCL ), B-4 (CLStructure of CLCL ), B-5 (CLStructure of CLCL ), B-6 (CLStructure of CLCL ), B-7 (CLStructure of CLCL ), B-8 (CLStructure of CLCL ), B-9 (CLStructure of CLCL ), C (CLStructure of CLCL ), C-1 (CLStructure of CLCL ), C-10 (CLStructure of CLCL ), C-11 (CLStructure of CLCL ), C-12 (CLStructure of CLCL ), C-13 (CLStructure of CLCL ), C-14 (CLStructure of CLCL ), C-15 (CLStructure of CLCL ), C-16 (CLStructure of CLCL ), C-17 (CLStructure of CLCL ), C-18 (CLStructure of CLCL ), C-19 (CLStructure of CLCL ), C-2 (CLStructure of CLCL ), C-20 (CLStructure of CLCL ), C-21 (CLStructure of CLCL ), C-22 (CLStructure of CLCL ), C-23 (CLStructure of CLCL ), C-3 (CLStructure of CLCL ), C-4 (CLStructure of CLCL ), C-5 (CLStructure of CLCL ), C-6 (CLStructure of CLCL ), C-7 (CLStructure of CLCL ), C-8 (CLStructure of CLCL ), C-9 (CLStructure of CLCL ), D (CLStructure of CLCL ), D-1 (CLStructure of CLCL ), D-10 (CLStructure of CLCL ), D-11 (CLStructure of CLCL ), D-12 (CLStructure of CLCL ), D-13 (CLStructure of CLCL ), D-14 (CLStructure of CLCL ), D-15 (CLStructure of CLCL ), D-16 (CLStructure of CLCL ), D-17 (CLStructure of CLCL ), D-18 (CLStructure of CLCL ), D-19 (CLStructure of CLCL ), D-2 (CLStructure of CLCL ), D-20 (CLStructure of CLCL ), D-21 (CLStructure of CLCL ), D-22 (CLStructure of CLCL ), D-23 (CLStructure of CLCL ), D-3 (CLStructure of CLCL ), D-4 (CLStructure of CLCL ), D-5 (CLStructure of CLCL ), D-6 (CLStructure of CLCL ), D-7 (CLStructure of CLCL ), D-8 (CLStructure of CLCL ), D-9 (CLStructure of CLCL ), E (CAStructure of CACA ), E-1 (CAStructure of CACA ), E-10 (CAStructure of CACA ), E-11 (CAStructure of CACA ), E-12 (CAStructure of CACA ), E-13 (CAStructure of CACA ), E-14 (CAStructure of CACA ), E-15 (CAStructure of CACA ), E-16 (CAStructure of CACA ), E-17 (CAStructure of CACA ), E-18 (CAStructure of CACA ), E-19 (CAStructure of CACA ), E-2 (CAStructure of CACA ), E-20 (CAStructure of CACA ), E-21 (CAStructure of CACA ), E-22 (CAStructure of CACA ), E-23 (CAStructure of CACA ), E-3 (CAStructure of CACA ), E-4 (CAStructure of CACA ), E-5 (CAStructure of CACA ), E-6 (CAStructure of CACA ), E-7 (CAStructure of CACA ), E-8 (CAStructure of CACA ), E-9 (CAStructure of CACA )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Chain A-1 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-1
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-10 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-10
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-11 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-11
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Chain A-12 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-13 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-1
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Chain A-14 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-3
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-15 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-2
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-16 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-10
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-17 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-11
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-18 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-9
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-19 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-8
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-2 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-2
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-20 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-7
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-21 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-6
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-22 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-4
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-23 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-5
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-3 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-3
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-4 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-4
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-5 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-5
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-6 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-6
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Chain A-7 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-7
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Chain A-8 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-8
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain A-9 heme  
auth_asym_id A
Residue indices (Uniprot) 2-160 (1-161)
Mutations (UniProt numbering)
Missing residues 75SER-75SER
Structural gaps Exists
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme F-9
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å