MolNFT v1 · #170588 · protein

Crystal structure of KRED1-pglu enzyme

6YC8 · Ketoreductase: “Crystal structure of KRED1-pglu enzyme”. X-ray diffraction, 1 ligand (NAP), 1 pocket (best druggability 0.78). MolNFT v1 #170588 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6YC8
Type: protein
Length: 240 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ketoreductase
UniProt: A0A0H4SN47
Ligands: NAP
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ketoreductase	protein	240	55% helix, 14% strand	A0A0H4SN47

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A
PGE · Triethylene glycol · additive · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A
ACT · Acetate ion · additive · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 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	359	0.78	0.88	48	NAP, ACT

Compared structures

6YC8 · Crystal structure of KRED1-Pglu enzyme · 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 A0A0H4SN47
Elsewhere: RCSB PDB 6YC8 · PDBe 6YC8 · UniProt A0A0H4SN47

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.