PDB ID:  pdb_00006udl
  • Structure of Human Cytochrome P450 1A1 with Duocarmycin Prodrug (S) ICT-2700
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.85 Å
  • Deposition date: 2019-09-19
Number of assemblies:  4
Assembly ID:  1  (author_defined_assembly)    
Structural data modeled
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others F (Q4MStructure of Q4MQ4M )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 36-512 (35-512)
Mutations (UniProt numbering)
Missing residues 293GLN-300VAL
Structural gaps Exists
Uniprot ID P04798 →UniprotKB
label_asym_ids of heme E
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Assembly ID:  2  (author_defined_assembly)    
Structural data PDB
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others H (Q4MStructure of Q4MQ4M )
Each chain information
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 36-512 (35-512)
Mutations (UniProt numbering)
Uniprot ID P04798 →UniprotKB
label_asym_ids of heme G
Available structure PDB
Assembly ID:  3  (author_defined_assembly)    
Structural data modeled
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others
Each chain information
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 36-512 (35-512)
Mutations (UniProt numbering)
Missing residues 291GLU-301GLN
Structural gaps Exists
Uniprot ID P04798 →UniprotKB
label_asym_ids of heme I
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Assembly ID:  4  (author_defined_assembly)    
Structural data modeled
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others
Each chain information
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 36-512 (35-512)
Mutations (UniProt numbering)
Missing residues 290GLN-301GLN
Structural gaps Exists
Uniprot ID P04798 →UniprotKB
label_asym_ids of heme J
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å