MolNFT v1 · #178943 · protein

Structure of wild type GLYOXYLATE/HYDROXYPYRUVATE reductase a from escherichia COLI in complex with alpha-ketoglutarate and NADP+

7JQI: “Structure of wild type GLYOXYLATE/HYDROXYPYRUVATE reductase a from escherichia COLI in complex with…”. X-ray diffraction, 2 ligands (AKG, NAP), 2 pockets (best druggability 0.74). MolNFT v1 #178943 on GenesisL1: 3D structure…

PDB: 7JQI
Type: protein
Length: 312 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GLYOXYLATE/HYDROXYPYRUVATE reductase a
EC: 1.1.1.79, 1.1.1.81
UniProt: A0A140NAE3
Ligands: AKG, NAP
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GLYOXYLATE/HYDROXYPYRUVATE reductase a (EC 1.1.1.79, 1.1.1.81)	protein	312	35% helix, 17% strand	A0A140NAE3

Ligands and binding sites

AKG · 2-oxoglutaric acid · ligand · chains A
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

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

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	501	0.74	0.83	60	AKG, NAP
2	70	0.31	0.74	15	empty

Compared structures

7JQI · Structure of wild type Glyoxylate/Hydroxypyruvate reductase A from Escherichia Coli in… · 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 A0A140NAE3
Elsewhere: RCSB PDB 7JQI · PDBe 7JQI · UniProt A0A140NAE3

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