MolNFT v1 · #25279 · protein

Crystal structure of a putative nitroreductase (TM1586) from thermotoga maritima MSB8 at 2.00 a resolution

1VKW: “Crystal structure of a putative nitroreductase (TM1586) from thermotoga maritima MSB8 at 2.00 a resolution”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.46). MolNFT v1 #25279 on GenesisL1: 3D structure, binding…

PDB: 1VKW
Type: protein
Length: 217 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative nitroreductase
UniProt: Q9X1S2
Ligands: SO4
Pockets: 3 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative nitroreductase	protein	217	35% helix, 18% strand	Q9X1S2

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	138	0.46	0.77	17	empty
2	95	0.38	0.76	20	SO4
3	58	0.35	0.78	12	empty

Modifications

Observed in the structure: 4 modified, 1 disulfide (engineered, disulfide).

Compared structures

1VKW · Crystal structure of a putative nitroreductase (tm1586) from thermotoga maritima msb8 at… · 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 Q9X1S2
Elsewhere: RCSB PDB 1VKW · PDBe 1VKW · UniProt Q9X1S2

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