Danish
PDB ID:  pdb_00003nod
  • MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER (DELTA 65) WITH TETRAHYDROBIOPTERIN AND PRODUCT ANALOGUE L-THIOCITRULLINE
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 2.7 Å
  • Deposition date: 1998-03-06
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 (SO4Structure of SO4SO4 ), C-1 (SO4Structure of SO4SO4 ), E (H4BStructure of H4BH4B ), E-1 (H4BStructure of H4BH4B ), F (SCIStructure of SCISCI ), F-1 (SCIStructure of SCISCI )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 77-496 (77-499)
Missing residues 102PHE-107LYS
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 0.10 Å
Chain A-1 heme  
auth_asym_id A
Residue indices (Uniprot) 77-496 (77-499)
Missing residues 102PHE-107LYS
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 0.13 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 (H4BStructure of H4BH4B ), H-1 (H4BStructure of H4BH4B ), I (SCIStructure of SCISCI ), I-1 (SCIStructure of SCISCI )
Each chain information
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 77-496 (77-499)
Missing residues 101ASP-107LYS
Structural gaps Exists
Uniprot ID P29477 ￫UniprotKB
label_asym_ids of heme G
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
Chain B-1 heme  
auth_asym_id B
Residue indices (Uniprot) 77-496 (77-499)
Missing residues 101ASP-107LYS
Structural gaps Exists
Uniprot ID P29477 ￫UniprotKB
label_asym_ids of heme G-1
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å