PDB ID:  pdb_00006n6q
  • Crystal structure of a Cytochrome P450 (CYP102L1)
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.5 Å
  • Deposition date: 2018-11-26
Number of assemblies:  4
Assembly ID:  1  (author_and_software_defined_assembly)    
Structural data PDB
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others F (CACStructure of CACCAC )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 37-482 (-)
Uniprot ID Unavailable
label_asym_ids of heme E
Available structure PDB
Assembly ID:  2  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others H (CACStructure of CACCAC ), I (CACStructure of CACCAC )
Each chain information
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 21-481 (-)
Missing residues 209ARG-221GLY
Structural gaps Exists
Uniprot ID Unavailable
label_asym_ids of heme G
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Assembly ID:  3  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others K (CACStructure of CACCAC )
Each chain information
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 37-482 (-)
Missing residues 220LEU-222GLY
Structural gaps Exists
Uniprot ID Unavailable
label_asym_ids of heme J
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å
Assembly ID:  4  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 1
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others M (CACStructure of CACCAC )
Each chain information
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 37-480 (-)
Missing residues 219PHE-222GLY
Structural gaps Exists
Uniprot ID Unavailable
label_asym_ids of heme L
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å