MolNFT v1 · #144241 · protein

Crystal structure of V278E-glyoxalase I mutant from zea mays in space group P4(1)2(1)2

6BNN · Lactoylglutathione lyase: “Crystal structure of V278E-glyoxalase I mutant from zea mays in space group P4(1)2(1)2”. X-ray diffraction, 2 ligands (GSH, CO), 2 pockets (best druggability 0.56). MolNFT v1 #144241 on GenesisL1: 3D…

PDB: 6BNN
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lactoylglutathione lyase
EC: 4.4.1.5
UniProt: B6TPH0
Ligands: GSH, CO
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lactoylglutathione lyase (EC 4.4.1.5)	protein	282	26% helix, 41% strand	B6TPH0

Ligands and binding sites

GSH · Glutathione · ligand · chains A
CO · Cobalt (II) ion · metal · chains A
FMT · Formic acid · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	246	0.56	0.77	27	GSH
2	267	0.55	0.76	24	empty

Compared structures

6BNN · Crystal structure of V278E-glyoxalase I mutant from Zea mays in space group P4(1)2(1)2 · 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 B6TPH0
Elsewhere: RCSB PDB 6BNN · PDBe 6BNN · UniProt B6TPH0

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