PDB ID:  pdb_00008fda
  • Human Cytochrome P450 17A1 in complex with steroidal isonitrile inhibitor
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.2 Å
  • Deposition date: 2022-12-02
Number of assemblies:  4
Assembly ID:  1  (author_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others F (XPKStructure of XPKXPK ), H (XPKStructure of XPKXPK )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 28-503 (24-508)
Mutations (UniProt numbering)
Missing residues 274ASP-282GLN
Structural gaps Exists
Uniprot ID P05093 →UniprotKB
label_asym_ids of heme E ,  E ,  E
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 30-503 (24-508)
Mutations (UniProt numbering)
Missing residues 274ASP-282GLN
Structural gaps Exists
Uniprot ID P05093 →UniprotKB
label_asym_ids of heme G ,  G
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Assembly ID:  2  (author_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others F (XPKStructure of XPKXPK ), J (XPKStructure of XPKXPK ), K (XPKStructure of XPKXPK )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 28-503 (24-508)
Mutations (UniProt numbering)
Missing residues 274ASP-282GLN
Structural gaps Exists
Uniprot ID P05093 →UniprotKB
label_asym_ids of heme E ,  E ,  E
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 30-504 (24-508)
Mutations (UniProt numbering)
Missing residues 275ASN-282GLN
Structural gaps Exists
Uniprot ID P05093 →UniprotKB
label_asym_ids of heme I ,  I
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Assembly ID:  3  (author_defined_assembly)    
Structural data modeled
Oligomeric count 3
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others F (XPKStructure of XPKXPK ), J (XPKStructure of XPKXPK ), K (XPKStructure of XPKXPK ), M (XPKStructure of XPKXPK ), N (XPKStructure of XPKXPK )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 28-503 (24-508)
Mutations (UniProt numbering)
Missing residues 274ASP-282GLN
Structural gaps Exists
Uniprot ID P05093 →UniprotKB
label_asym_ids of heme E ,  E ,  E
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) 30-504 (24-508)
Mutations (UniProt numbering)
Missing residues 275ASN-282GLN
Structural gaps Exists
Uniprot ID P05093 →UniprotKB
label_asym_ids of heme I ,  I
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 31-503 (24-508)
Mutations (UniProt numbering)
Missing residues 275ASN-281ASP
Structural gaps Exists
Uniprot ID P05093 →UniprotKB
label_asym_ids of heme L ,  L
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Assembly ID:  4  (author_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others H (XPKStructure of XPKXPK ), M (XPKStructure of XPKXPK ), N (XPKStructure of XPKXPK )
Each chain information
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 30-503 (24-508)
Mutations (UniProt numbering)
Missing residues 274ASP-282GLN
Structural gaps Exists
Uniprot ID P05093 →UniprotKB
label_asym_ids of heme G ,  G
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 31-503 (24-508)
Mutations (UniProt numbering)
Missing residues 275ASN-281ASP
Structural gaps Exists
Uniprot ID P05093 →UniprotKB
label_asym_ids of heme L ,  L
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å