Research workbench

Human inducible nitric oxide synthase, zn-free, seitu complex

Analyse Human inducible nitric oxide synthase, zn-free, seitu complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NSI
Type: protein
Length: 1,680 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (nitric oxide synthase)
EC: 1.14.13.39
UniProt: P35228
Ligands: HEM, H4B, ITU, SO4
Pockets: 20 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Protein (nitric oxide synthase) (EC 1.14.13.39)	protein	420	40% helix, 15% strand	P35228

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
H4B · 5,6,7,8-tetrahydrobiopterin · ligand · 4 copies · chains A, B, C, D
ITU · Ethylisothiourea · ligand · 4 copies · chains A, B, C, D
SO4 · Sulfate ion · ion · 9 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1117	0.87	0.88	112	HEM, H4B, ITU
2	1095	0.84	0.85	77	HEM, H4B, ITU
3	280	0.84	0.95	56	H4B
4	202	0.77	0.92	34	HEM, ITU
5	182	0.76	0.91	34	HEM, ITU

Interfaces

3 interfaces between chains.

C–D · 2679 Å² buried · 29 hydrogen bonds · protein-protein
A–B · 2654 Å² buried · 33 hydrogen bonds · protein-protein
B–C · 652 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2NSI · Human inducible nitric oxide synthase, zn-free, seitu complex · the same entry in another collection · chain A against A, TM-score 1.00
P35228 · AlphaFold monomer V2.0 prediction for nitric oxide synthase, inducible (P35228) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P35228
Elsewhere: RCSB PDB 2NSI · PDBe 2NSI · UniProt P35228

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.