PDB ID:  pdb_00001jwk
  • Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with W457A Mutation at Tetrahydrobiopterin Binding Site
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.3 Å
  • Deposition date: 2001-09-04
Number of assemblies:  2
Assembly ID:  1  (author_and_software_defined_assembly)    
Structural data modeled
Oligomeric count 2
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others C (BOGStructure of BOGBOG ), C-1 (BOGStructure of BOGBOG ), E (HBIStructure of HBIHBI ), E-1 (HBIStructure of HBIHBI ), F (EDOStructure of EDOEDO ), F-1 (EDOStructure of EDOEDO ), G (GOLStructure of GOLGOL ), G-1 (GOLStructure of GOLGOL )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 77-497 (101-498)
Mutations (UniProt numbering)
Missing residues 100SER-108LYS
Structural gaps Exists
Uniprot ID P29477 →UniprotKB
label_asym_ids of heme D
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.09 Å
Chain A-1 heme  
auth_asym_id A
Residue indices (Uniprot) 77-497 (101-498)
Mutations (UniProt numbering)
Missing residues 100SER-108LYS
Structural gaps Exists
Uniprot ID P29477 →UniprotKB
label_asym_ids of heme D-1
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.09 Å
Assembly ID:  2  (author_and_software_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 (BOGStructure of BOGBOG ), H-1 (BOGStructure of BOGBOG ), J (HBIStructure of HBIHBI ), J-1 (HBIStructure of HBIHBI ), K (EDOStructure of EDOEDO ), K-1 (EDOStructure of EDOEDO )
Each chain information
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 77-497 (66-100)
Mutations (UniProt numbering)
Missing residues 100SER-109SER
Structural gaps Exists
Uniprot ID P29477 →UniprotKB
label_asym_ids of heme I
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å
Chain B-1 heme  
auth_asym_id B
Residue indices (Uniprot) 77-497 (66-100)
Mutations (UniProt numbering)
Missing residues 100SER-109SER
Structural gaps Exists
Uniprot ID P29477 →UniprotKB
label_asym_ids of heme I-1
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.09 Å