Danish
PDB ID:  pdb_00008sqt
  • Crystal Structure of Bacterioferritin (Bfr) from Brucella abortus (iron bound, cubic form 2, F16L mutant)
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.2 Å
  • Deposition date: 2023-05-04
Number of assemblies:  1
Assembly ID:  1  (author_and_software_defined_assembly)    
Structural data PDB
Oligomeric count 24
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others B (SO4Structure of SO4SO4 ), B-1 (SO4Structure of SO4SO4 ), B-10 (SO4Structure of SO4SO4 ), B-11 (SO4Structure of SO4SO4 ), B-12 (SO4Structure of SO4SO4 ), B-13 (SO4Structure of SO4SO4 ), B-14 (SO4Structure of SO4SO4 ), B-15 (SO4Structure of SO4SO4 ), B-16 (SO4Structure of SO4SO4 ), B-17 (SO4Structure of SO4SO4 ), B-18 (SO4Structure of SO4SO4 ), B-19 (SO4Structure of SO4SO4 ), B-2 (SO4Structure of SO4SO4 ), B-20 (SO4Structure of SO4SO4 ), B-21 (SO4Structure of SO4SO4 ), B-22 (SO4Structure of SO4SO4 ), B-23 (SO4Structure of SO4SO4 ), B-3 (SO4Structure of SO4SO4 ), B-4 (SO4Structure of SO4SO4 ), B-5 (SO4Structure of SO4SO4 ), B-6 (SO4Structure of SO4SO4 ), B-7 (SO4Structure of SO4SO4 ), B-8 (SO4Structure of SO4SO4 ), B-9 (SO4Structure of SO4SO4 ), C (SO4Structure of SO4SO4 ), C-1 (SO4Structure of SO4SO4 ), C-10 (SO4Structure of SO4SO4 ), C-11 (SO4Structure of SO4SO4 ), C-12 (SO4Structure of SO4SO4 ), C-13 (SO4Structure of SO4SO4 ), C-14 (SO4Structure of SO4SO4 ), C-15 (SO4Structure of SO4SO4 ), C-16 (SO4Structure of SO4SO4 ), C-17 (SO4Structure of SO4SO4 ), C-18 (SO4Structure of SO4SO4 ), C-19 (SO4Structure of SO4SO4 ), C-2 (SO4Structure of SO4SO4 ), C-20 (SO4Structure of SO4SO4 ), C-21 (SO4Structure of SO4SO4 ), C-22 (SO4Structure of SO4SO4 ), C-23 (SO4Structure of SO4SO4 ), C-3 (SO4Structure of SO4SO4 ), C-4 (SO4Structure of SO4SO4 ), C-5 (SO4Structure of SO4SO4 ), C-6 (SO4Structure of SO4SO4 ), C-7 (SO4Structure of SO4SO4 ), C-8 (SO4Structure of SO4SO4 ), C-9 (SO4Structure of SO4SO4 ), 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 (CLStructure of CLCL ), E-1 (CLStructure of CLCL ), E-10 (CLStructure of CLCL ), E-11 (CLStructure of CLCL ), E-12 (CLStructure of CLCL ), E-13 (CLStructure of CLCL ), E-14 (CLStructure of CLCL ), E-15 (CLStructure of CLCL ), E-16 (CLStructure of CLCL ), E-17 (CLStructure of CLCL ), E-18 (CLStructure of CLCL ), E-19 (CLStructure of CLCL ), E-2 (CLStructure of CLCL ), E-20 (CLStructure of CLCL ), E-21 (CLStructure of CLCL ), E-22 (CLStructure of CLCL ), E-23 (CLStructure of CLCL ), E-3 (CLStructure of CLCL ), E-4 (CLStructure of CLCL ), E-5 (CLStructure of CLCL ), E-6 (CLStructure of CLCL ), E-7 (CLStructure of CLCL ), E-8 (CLStructure of CLCL ), E-9 (CLStructure of CLCL ), F (FE2Structure of FE2FE2 ), F-1 (FE2Structure of FE2FE2 ), F-10 (FE2Structure of FE2FE2 ), F-11 (FE2Structure of FE2FE2 ), F-12 (FE2Structure of FE2FE2 ), F-13 (FE2Structure of FE2FE2 ), F-14 (FE2Structure of FE2FE2 ), F-15 (FE2Structure of FE2FE2 ), F-16 (FE2Structure of FE2FE2 ), F-17 (FE2Structure of FE2FE2 ), F-18 (FE2Structure of FE2FE2 ), F-19 (FE2Structure of FE2FE2 ), F-2 (FE2Structure of FE2FE2 ), F-20 (FE2Structure of FE2FE2 ), F-21 (FE2Structure of FE2FE2 ), F-22 (FE2Structure of FE2FE2 ), F-23 (FE2Structure of FE2FE2 ), F-3 (FE2Structure of FE2FE2 ), F-4 (FE2Structure of FE2FE2 ), F-5 (FE2Structure of FE2FE2 ), F-6 (FE2Structure of FE2FE2 ), F-7 (FE2Structure of FE2FE2 ), F-8 (FE2Structure of FE2FE2 ), F-9 (FE2Structure of FE2FE2 ), G (FE2Structure of FE2FE2 ), G-1 (FE2Structure of FE2FE2 ), G-10 (FE2Structure of FE2FE2 ), G-11 (FE2Structure of FE2FE2 ), G-12 (FE2Structure of FE2FE2 ), G-13 (FE2Structure of FE2FE2 ), G-14 (FE2Structure of FE2FE2 ), G-15 (FE2Structure of FE2FE2 ), G-16 (FE2Structure of FE2FE2 ), G-17 (FE2Structure of FE2FE2 ), G-18 (FE2Structure of FE2FE2 ), G-19 (FE2Structure of FE2FE2 ), G-2 (FE2Structure of FE2FE2 ), G-20 (FE2Structure of FE2FE2 ), G-21 (FE2Structure of FE2FE2 ), G-22 (FE2Structure of FE2FE2 ), G-23 (FE2Structure of FE2FE2 ), G-3 (FE2Structure of FE2FE2 ), G-4 (FE2Structure of FE2FE2 ), G-5 (FE2Structure of FE2FE2 ), G-6 (FE2Structure of FE2FE2 ), G-7 (FE2Structure of FE2FE2 ), G-8 (FE2Structure of FE2FE2 ), G-9 (FE2Structure of FE2FE2 ), H (FE2Structure of FE2FE2 ), H-1 (FE2Structure of FE2FE2 ), H-10 (FE2Structure of FE2FE2 ), H-11 (FE2Structure of FE2FE2 ), H-12 (FE2Structure of FE2FE2 ), H-13 (FE2Structure of FE2FE2 ), H-14 (FE2Structure of FE2FE2 ), H-15 (FE2Structure of FE2FE2 ), H-16 (FE2Structure of FE2FE2 ), H-17 (FE2Structure of FE2FE2 ), H-18 (FE2Structure of FE2FE2 ), H-19 (FE2Structure of FE2FE2 ), H-2 (FE2Structure of FE2FE2 ), H-20 (FE2Structure of FE2FE2 ), H-21 (FE2Structure of FE2FE2 ), H-22 (FE2Structure of FE2FE2 ), H-23 (FE2Structure of FE2FE2 ), H-3 (FE2Structure of FE2FE2 ), H-4 (FE2Structure of FE2FE2 ), H-5 (FE2Structure of FE2FE2 ), H-6 (FE2Structure of FE2FE2 ), H-7 (FE2Structure of FE2FE2 ), H-8 (FE2Structure of FE2FE2 ), H-9 (FE2Structure of FE2FE2 )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I
Available structure PDB
Chain A-1 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-1
Available structure PDB
Chain A-10 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-10
Available structure PDB
Chain A-11 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-11
Available structure PDB
Chain A-12 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I
Available structure PDB
Chain A-13 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-1
Available structure PDB
Chain A-14 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-3
Available structure PDB
Chain A-15 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-2
Available structure PDB
Chain A-16 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-10
Available structure PDB
Chain A-17 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-11
Available structure PDB
Chain A-18 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-9
Available structure PDB
Chain A-19 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-8
Available structure PDB
Chain A-2 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-2
Available structure PDB
Chain A-20 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-7
Available structure PDB
Chain A-21 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-6
Available structure PDB
Chain A-22 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-4
Available structure PDB
Chain A-23 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-5
Available structure PDB
Chain A-3 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-3
Available structure PDB
Chain A-4 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-4
Available structure PDB
Chain A-5 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-5
Available structure PDB
Chain A-6 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-6
Available structure PDB
Chain A-7 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-7
Available structure PDB
Chain A-8 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-8
Available structure PDB
Chain A-9 heme  
auth_asym_id A
Residue indices (Uniprot) 0-159 (1-161)
Mutations (UniProt numbering)
Uniprot ID Q2YKI4 ￫UniprotKB
label_asym_ids of heme I-9
Available structure PDB