PDB ID:  pdb_00004d1o
  • Structure of human endothelial nitric oxide synthase heme domain with L-Arg bound
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 1.819 Å
  • Deposition date: 2014-05-02
Number of assemblies:  1
Assembly ID:  0  (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 (ARGStructure of ARGARG ), E (ACTStructure of ACTACT ), F (BTBStructure of BTBBTB ), G (BTBStructure of BTBBTB ), H (GOLStructure of GOLGOL ), I (GOLStructure of GOLGOL ), J (ZNStructure of ZNZN ), K (H4BStructure of H4BH4B ), L (GDStructure of GDGD ), M (ARGStructure of ARGARG ), O (ACTStructure of ACTACT ), P (BTBStructure of BTBBTB ), Q (BTBStructure of BTBBTB ), R (GOLStructure of GOLGOL ), S (H4BStructure of H4BH4B ), T (GDStructure of GDGD )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 68-480 (41-480)
Mutations (UniProt numbering)
Missing residues 107ARG-118PRO
Structural gaps Exists
Uniprot ID P29474 →UniprotKB
label_asym_ids of heme D
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 67-480 (41-480)
Mutations (UniProt numbering)
Missing residues 107ARG-118PRO
Structural gaps Exists
Uniprot ID P29474 →UniprotKB
label_asym_ids of heme N
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å