Research workbench

Crystal structure of glyoxalase I from zea mays

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

PDB: 5D7Z
Type: protein
Length: 281 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: NI, NA
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lactoylglutathione lyase (EC 4.4.1.5)	protein	281	26% helix, 40% strand	B6TPH0

Ligands and binding sites

NI · Nickel (II) ion · metal · chains A
NA · Sodium ion · metal
FMT · Formic acid · additive · 5 copies · chains A
2PE · Nonaethylene glycol · additive · 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	262	0.56	0.77	26	FMT
2	169	0.45	0.75	22	FMT, NA, 2PE

Compared structures

5D7Z · Crystal structure of glyoxalase I from Zea mays · 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 5D7Z · PDBe 5D7Z · UniProt B6TPH0

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