Danish
PDB ID:  pdb_00001ppj
  • Bovine cytochrome bc1 complex with stigmatellin and antimycin
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.1 Å
  • Deposition date: 2003-06-16
Number of assemblies:  1
Assembly ID:  0  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 20
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others AA (AZIStructure of AZIAZI ), AB (SMAStructure of SMASMA ), BA (PO4Structure of PO4PO4 ), BB (CDLStructure of CDLCDL ), CB (PEEStructure of PEEPEE ), DB (ANYStructure of ANYANY ), EA (SMAStructure of SMASMA ), EB (GOLStructure of GOLGOL ), FA (PEEStructure of PEEPEE ), GA (ANYStructure of ANYANY ), GB (PEEStructure of PEEPEE ), HA (GOLStructure of GOLGOL ), HB (JZRStructure of JZRJZR ), IA (GOLStructure of GOLGOL ), IB (FESStructure of FESFES ), JA (JZRStructure of JZRJZR ), JB (GOLStructure of GOLGOL ), KB (JZRStructure of JZRJZR ), LA (CDLStructure of CDLCDL ), LB (PO4Structure of PO4PO4 ), MA (PEEStructure of PEEPEE ), MB (CDLStructure of CDLCDL ), NA (FESStructure of FESFES ), OA (JZRStructure of JZRJZR ), PA (JZRStructure of JZRJZR ), QA (PO4Structure of PO4PO4 ), RA (AZIStructure of AZIAZI ), SA (CDLStructure of CDLCDL ), TA (AZIStructure of AZIAZI ), U (JZRStructure of JZRJZR ), UA (GOLStructure of GOLGOL ), V (PO4Structure of PO4PO4 ), VA (JZRStructure of JZRJZR ), W (AZIStructure of AZIAZI ), WA (AZIStructure of AZIAZI ), X (GOLStructure of GOLGOL ), XA (PO4Structure of PO4PO4 ), Y (JZRStructure of JZRJZR ), Z (JZRStructure of JZRJZR )
Each chain information

Showing all 20 chains (4 with heme). Show only chains with heme

Chain A  
auth_asym_id A
Residue indices (Uniprot) 2-442 (35-480)
Uniprot ID P31800 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB
Chain B  
auth_asym_id B
Residue indices (Uniprot) 12-439 (15-453)
Missing residues 13ALA-16GLY:20HIS-20HIS:231GLY-231GLY
Structural gaps Exists
Uniprot ID P23004 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 15-379 (1-379)
Uniprot ID P00157 ￫UniprotKB
label_asym_ids of heme CA ,  DA
Available structure PDB
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 1-241 (85-325)
Uniprot ID P00125 ￫UniprotKB
label_asym_ids of heme KA
Available structure PDB
Chain E  
auth_asym_id E
Residue indices (Uniprot) 1-196 (79-274)
Uniprot ID P13272 ￫UniprotKB
S-S bonds 144:160
label_asym_ids of heme None
Available structure PDB
Chain F  
auth_asym_id F
Residue indices (Uniprot) 12-110 (2-111)
Mutations (UniProt numbering)
Uniprot ID P00129 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB
Chain G  
auth_asym_id G
Residue indices (Uniprot) 2-74 (2-82)
Uniprot ID P13271 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB
Chain H  
auth_asym_id H
Residue indices (Uniprot) 13-78 (14-91)
Uniprot ID P00126 ￫UniprotKB
S-S bonds 24:68,40:54
label_asym_ids of heme None
Available structure PDB
Chain I  
auth_asym_id I
Residue indices (Uniprot) 32-78 (1-78)
Mutations (UniProt numbering)
Missing residues 44ASP-48SER
Structural gaps Exists
Uniprot ID P13272 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.28 Å
Chain J  
auth_asym_id J
Residue indices (Uniprot) 30-62 (2-63)
Missing residues 61ASN-61ASN
Structural gaps Exists
Uniprot ID P00130 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.16 Å
Chain K  
auth_asym_id N
Residue indices (Uniprot) 2-442 (35-480)
Uniprot ID P31800 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB
Chain L  
auth_asym_id O
Residue indices (Uniprot) 12-439 (15-453)
Missing residues 13ALA-16GLY:20HIS-20HIS:305GLN-305GLN
Structural gaps Exists
Uniprot ID P23004 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å
Chain M heme  
auth_asym_id P
Residue indices (Uniprot) 16-379 (1-379)
Uniprot ID P00157 ￫UniprotKB
label_asym_ids of heme YA ,  ZA
Available structure PDB
Chain N heme  
auth_asym_id Q
Residue indices (Uniprot) 1-241 (85-325)
Uniprot ID P00125 ￫UniprotKB
label_asym_ids of heme FB
Available structure PDB
Chain O  
auth_asym_id R
Residue indices (Uniprot) 1-196 (79-274)
Uniprot ID P13272 ￫UniprotKB
S-S bonds 144:160
label_asym_ids of heme None
Available structure PDB
Chain P  
auth_asym_id S
Residue indices (Uniprot) 12-110 (2-111)
Mutations (UniProt numbering)
Uniprot ID P00129 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB
Chain Q  
auth_asym_id T
Residue indices (Uniprot) 2-75 (2-82)
Uniprot ID P13271 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB
Chain R  
auth_asym_id U
Residue indices (Uniprot) 13-78 (14-91)
Uniprot ID P00126 ￫UniprotKB
S-S bonds 24:68,40:54
label_asym_ids of heme None
Available structure PDB
Chain S  
auth_asym_id V
Residue indices (Uniprot) 32-78 (1-78)
Mutations (UniProt numbering)
Missing residues 44ASP-48SER
Structural gaps Exists
Uniprot ID P13272 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.24 Å
Chain T  
auth_asym_id W
Residue indices (Uniprot) 1-62 (2-63)
Missing residues 61ASN-61ASN
Structural gaps Exists
Uniprot ID P00130 ￫UniprotKB
label_asym_ids of heme None
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.15 Å