PDB ID:  pdb_00009q4h
  • Structure of human neuronal nitric oxide synthase R354A/G357D mutant heme domain bound with 6-((2,3-difluoro-5-(2-(methylamino)ethyl)phenoxy)methyl)-4-methylpyridin-2-amine
  • Experimental method: X-RAY DIFFRACTION
  • Resolution: 1.99 Å
  • Deposition date: 2025-08-20
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 F (H4BStructure of H4BH4B ), G (A1CStructure of A1CA1C ), H (GOLStructure of GOLGOL ), I (GOLStructure of GOLGOL ), J (H4BStructure of H4BH4B ), K (ZNStructure of ZNZN ), M (A1CStructure of A1CA1C )
Each chain information
Chain A heme  
auth_asym_id A
Residue indices (Uniprot) 304-722 (302-722)
Mutations (UniProt numbering)
Missing residues 344SER-348ARG
Structural gaps Exists
Uniprot ID P29475 →UniprotKB
label_asym_ids of heme E
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
Chain B heme  
auth_asym_id B
Residue indices (Uniprot) 304-722 (302-722)
Mutations (UniProt numbering)
Uniprot ID P29475 →UniprotKB
label_asym_ids of heme L
Available structure PDB
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 O (A1CStructure of A1CA1C ), P (GOLStructure of GOLGOL ), Q (ZNStructure of ZNZN ), R (H4BStructure of H4BH4B ), T (H4BStructure of H4BH4B ), U (A1CStructure of A1CA1C ), V (GOLStructure of GOLGOL )
Each chain information
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 303-722 (302-722)
Mutations (UniProt numbering)
Uniprot ID P29475 →UniprotKB
label_asym_ids of heme N
Available structure PDB
Chain D heme  
auth_asym_id D
Residue indices (Uniprot) 303-722 (302-722)
Mutations (UniProt numbering)
Missing residues 345GLN-352ASP
Structural gaps Exists
Uniprot ID P29475 →UniprotKB
label_asym_ids of heme S
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å