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Crystal structure of mouse nitrilase-2 at 1.4A resolution

Analyse Crystal structure of mouse nitrilase-2 at 1.4A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W1V
Type: protein
Length: 548 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitrilase homolog 2
EC: 3.5.-.-
UniProt: Q9JHW2
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Nitrilase homolog 2 (EC 3.5.-.-)	protein	274	30% helix, 30% strand	Q9JHW2

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	81	0.63	0.90	20	empty
2	89	0.61	0.88	20	empty

Interfaces

1 interface between chains.

A–B · 2138 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

2W1V · Crystal structure of mouse nitrilase-2 at 1.4A resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q9JHW2 · AlphaFold monomer V2.0 prediction for omega-amidase NIT2 (Q9JHW2) · 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 Q9JHW2
Elsewhere: RCSB PDB 2W1V · PDBe 2W1V · UniProt Q9JHW2

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