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Structure of A1-type ketoreductase

Analyse Structure of A1-type ketoreductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DIF
Type: protein
Length: 952 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amphb
EC: 1.1.1.100
UniProt: Q93NW7
Ligands: NDP
Pockets: 10 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Amphb (EC 1.1.1.100)	protein	476	43% helix, 21% strand	Q93NW7

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · chains B

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

Pockets

10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	565	0.77	0.84	59	NDP
2	1165	0.75	0.78	128	empty
3	459	0.75	0.84	51	NDP
4	306	0.68	0.83	49	empty
5	58	0.62	0.92	19	empty

Interfaces

1 interface between chains.

A–B · 500 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4DIF · Structure of A1-type ketoreductase · 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 Q93NW7
Elsewhere: RCSB PDB 4DIF · PDBe 4DIF · UniProt Q93NW7

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