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Crystal structure of human glyoxalase domain-containing protein 4 (GLOD4)

Analyse Crystal structure of human glyoxalase domain-containing protein 4 (GLOD4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZI1
Type: protein
Length: 274 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glyoxalase domain-containing protein 4
UniProt: Q9HC38
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glyoxalase domain-containing protein 4	protein	274	22% helix, 39% strand	Q9HC38

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 4 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	306	0.63	0.79	32	EDO
2	76	0.63	0.90	18	empty
3	91	0.36	0.75	24	EDO
4	56	0.27	0.73	13	empty

Compared structures

3ZI1 · Crystal structure of human glyoxalase domain-containing protein 4 (GLOD4) · the same entry in another collection · chain A against A, TM-score 1.00
Q9HC38 · AlphaFold monomer V2.0 prediction for glyoxalase domain-containing protein 4 (Q9HC38) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9HC38
Elsewhere: RCSB PDB 3ZI1 · PDBe 3ZI1 · UniProt Q9HC38

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