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Structure-function study of AKR4C14, an aldo-keto reductase from thai jasmine rice (oryza sativa L. ssp. indica cv. KDML105)

Analyse Structure-function study of AKR4C14, an aldo-keto reductase from thai jasmine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KBL
Type: protein
Length: 314 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aldo-keto reductase
UniProt: B8AC38
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aldo-keto reductase	protein	314	43% helix, 16% strand	B8AC38

Ligands and binding sites

CAC · Cacodylate ion · additive · chains A
ACT · Acetate ion · additive · chains A
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	216	0.59	0.80	41	CAC, ACT, GOL
2	64	0.34	0.76	18	empty
3	58	0.29	0.74	13	empty

Compared structures

6KBL · Structure-function study of AKR4C14, an aldo-keto reductase from Thai Jasmine rice (Oryza… · 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 B8AC38
Elsewhere: RCSB PDB 6KBL · PDBe 6KBL · UniProt B8AC38

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