Research workbench

Crystal structure of 2-haloacrylate reductase

Analyse Crystal structure of 2-haloacrylate reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WLY
Type: protein
Length: 322 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2-haloacrylate reductase
EC: 1.-.-.-
UniProt: Q59I44
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2-haloacrylate reductase (EC 1.-.-.-)	protein	322	34% helix, 27% strand	Q59I44

Pockets

2 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	534	0.64	0.76	51	empty
2	63	0.31	0.75	15	empty

Compared structures

1WLY · Crystal Structure of 2-Haloacrylate Reductase · the same entry in another collection · chain A against A, TM-score 1.00
Q59I44 · AlphaFold monomer V2.0 prediction for 2-haloacrylate reductase (Q59I44) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 Q59I44
Elsewhere: RCSB PDB 1WLY · PDBe 1WLY · UniProt Q59I44

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