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Crystal structure of the NI(II)-bound Glyoxalase-I from Clostridium acetobutylicum

Analyse Crystal structure of the NI(II)-bound Glyoxalase-I from Clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HDP
Type: protein
Length: 132 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.06
Source: Clostridium acetobutylicum
Molecule: Glyoxalase-I
EC: 4.4.1.5
UniProt: Q97H22
Ligands: NI
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · resolution 2.06 · 1 distinct chain · 19% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glyoxalase-I (EC 4.4.1.5)	protein	132	19% helix, 47% strand	Q97H22

Ligands and binding sites

NI · Nickel (II) ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	206	0.59	0.80	27	empty

Compared structures

3HDP · Crystal structure of the NI(II)-bound glyoxalase-I from clostridium acetobutylicum · 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 Q97H22
Elsewhere: RCSB PDB 3HDP · PDBe 3HDP · UniProt Q97H22

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