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Crystal structure of the P332G mutant of the bacillus subtilis nos

Analyse Crystal structure of the P332G mutant of the bacillus subtilis nos in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AN0
Type: protein
Length: 361 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitric oxide synthase
EC: 1.14.13.39
UniProt: O34453
Ligands: HEM
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitric oxide synthase (EC 1.14.13.39)	protein	361	42% helix, 14% strand	O34453

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A

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

Pockets

3 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	650	0.78	0.83	52	HEM
2	103	0.42	0.77	19	empty
3	91	0.38	0.76	17	empty

Compared structures

2AN0 · Crystal Structure of the P332G mutant of the Bacillus subtilis NOS · the same entry in another collection · chain A against A, TM-score 1.00
O34453 · AlphaFold monomer V2.0 prediction for nitric oxide synthase oxygenase (O34453) · a predicted model of the same protein · 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 O34453
Elsewhere: RCSB PDB 2AN0 · PDBe 2AN0 · UniProt O34453

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