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Rat neuronal nitric oxide synthase oxygenase domain

Analyse Rat neuronal nitric oxide synthase oxygenase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZVI
Type: protein
Length: 417 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitric-oxide synthase, brain
EC: 1.14.13.39
UniProt: P29476
Ligands: HEM, H4B, ZN
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitric-oxide synthase, brain (EC 1.14.13.39)	protein	417	39% helix, 15% strand	P29476

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
H4B · 5,6,7,8-tetrahydrobiopterin · ligand · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	837	0.79	0.82	64	ZN, HEM, H4B
2	192	0.54	0.79	31	empty
3	70	0.51	0.85	15	empty
4	79	0.38	0.77	14	empty

Compared structures

1ZVI · Rat Neuronal Nitric Oxide Synthase Oxygenase Domain · 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 P29476
Elsewhere: RCSB PDB 1ZVI · PDBe 1ZVI · UniProt P29476

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