MolNFT v1 · #111750 · protein

Crystal structure of a probable lactoylglutathione lyase from brucella melitensis in complex with glutathione

4Z04 · GLYOXALASE/BLEOMYCIN resistance /dioxygenase superfamily…: “Crystal structure of a probable lactoylglutathione lyase from brucella melitensis in complex with glutathione”. X-ray diffraction, 2 ligands (GSH, ZN), 1 pocket (best…

PDB: 4Z04
Type: protein
Length: 124 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GLYOXALASE/BLEOMYCIN resistance /dioxygenase superfamily protein
UniProt: Q2YLQ3
Ligands: GSH, ZN
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GLYOXALASE/BLEOMYCIN resistance /dioxygenase superfamily protein	protein	124	23% helix, 34% strand	Q2YLQ3

Ligands and binding sites

GSH · Glutathione · ligand · chains A
ZN · Zinc ion · metal · chains A
MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	114	0.46	0.78	19	empty

Compared structures

4Z04 · Crystal structure of a probable lactoylglutathione lyase from Brucella melitensis 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 Q2YLQ3
Elsewhere: RCSB PDB 4Z04 · PDBe 4Z04 · UniProt Q2YLQ3

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