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Murine inducible nitric oxide synthase oxygenase domain (delta 114), aminoguanidine complex

Analyse Murine inducible nitric oxide synthase oxygenase domain (delta 114)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NOS
Type: protein
Length: 322 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inducible nitric oxide synthase
EC: 1.14.13.39
UniProt: P29477
Ligands: HEM, AGU
Pockets: 6 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Inducible nitric oxide synthase (EC 1.14.13.39)	protein	322	35% helix, 16% strand	P29477

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
AGU · Aminoguanidine · ligand · chains A
IMD · Imidazole · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	402	0.67	0.80	41	HEM, IMD, AGU
2	87	0.43	0.79	14	empty
3	142	0.42	0.75	21	empty
4	131	0.41	0.75	22	empty
5	72	0.39	0.79	25	empty

Compared structures

2NOS · Murine inducible nitric oxide synthase oxygenase domain (delta 114), aminoguanidine… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P29477
Elsewhere: RCSB PDB 2NOS · PDBe 2NOS · UniProt P29477

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