Research workbench

Clostridium beijerinckii aldo-keto reductase CBEI_3974 with NADPH

Analyse Clostridium beijerinckii aldo-keto reductase CBEI_3974 with NADPH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HG6
Type: protein
Length: 313 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-glyceraldehyde 3-phosphate reductase
EC: 1.1.1.-
UniProt: A0A1S8QGT2
Ligands: NDP
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-glyceraldehyde 3-phosphate reductase (EC 1.1.1.-)	protein	313	42% helix, 16% strand	A0A1S8QGT2

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
EDO · 1,2-ethanediol · additive · 8 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	289	0.61	0.79	34	NDP

Compared structures

6HG6 · Clostridium beijerinckii aldo-keto reductase Cbei_3974 with NADPH · 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 A0A1S8QGT2
Elsewhere: RCSB PDB 6HG6 · PDBe 6HG6 · UniProt A0A1S8QGT2

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