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Crystal structure of E144Q-glyoxalase I mutant from zea mays in space group P4(1)2(1)2

Analyse Crystal structure of E144Q-glyoxalase I mutant from zea mays in space group… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BNZ
Type: protein
Length: 277 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: 3 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lactoylglutathione lyase (EC 4.4.1.5)	protein	277	23% helix, 40% strand	B6TPH0

Ligands and binding sites

GSH · Glutathione · ligand · chains A
CO · Cobalt (II) ion · metal · chains A
FMT · Formic acid · additive · 5 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	317	0.60	0.78	29	FMT
2	281	0.60	0.78	30	GSH
3	53	0.30	0.76	13	empty

Compared structures

6BNZ · Crystal structure of E144Q-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 6BNZ · PDBe 6BNZ · UniProt B6TPH0

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