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Crystal structure of the Q18CP6_CLOD6 protein from glyoxalase family. northeast structural genomics consortium target CFR3

Analyse Crystal structure of the Q18CP6_CLOD6 protein from glyoxalase family. northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NVS
Type: protein
Length: 313 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative enzyme, glyoxalase family
UniProt: Q18CP6
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative enzyme, glyoxalase family	protein	156	37% helix, 29% strand	Q18CP6
B	Putative enzyme, glyoxalase family	protein	157	37% helix, 31% strand	Q18CP6

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.75	0.97	26	empty
2	297	0.68	0.82	40	empty
3	308	0.66	0.81	38	empty

Interfaces

1 interface between chains.

A–B · 1898 Å² buried · 28 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

4NVS · Crystal Structure of the Q18CP6_CLOD6 protein from glyoxalase family. Northeast… · 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 Q18CP6
Elsewhere: RCSB PDB 4NVS · PDBe 4NVS · UniProt Q18CP6

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