MolNFT v1 · #159849 · protein

2.5 ångström structure of wild type GLYOXYLATE/HYDROXYPYRUVATE reductase a from escherichia COLI in complex with 2-keto arginine and NADP

6P35: “2.5 ångström structure of wild type GLYOXYLATE/HYDROXYPYRUVATE reductase a from escherichia COLI in complex…”. X-ray diffraction, 3 ligands (NWG, NAP, SO4), 2 pockets (best druggability 0.73). MolNFT v1 #159849 on GenesisL1: 3D…

PDB: 6P35
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: NWG, NAP, SO4
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 34% 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	34% helix, 17% strand	A0A140NAE3

Ligands and binding sites

NWG · 5-[(diaminomethylidene)amino]-2-oxopentanoic acid · ligand · 2 copies · chains A
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A
GOL · Glycerol · additive · 2 copies · 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	514	0.73	0.82	61	NWG, NAP
2	57	0.26	0.73	15	empty

Compared structures

6P35 · 2.5 Angstrom structure of wild type Glyoxylate/Hydroxypyruvate reductase A from… · 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 6P35 · PDBe 6P35 · UniProt A0A140NAE3

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