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Crystal structure of ges-5 carbapenemase

Analyse Crystal structure of ges-5 carbapenemase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GNU
Type: protein
Length: 530 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase ges-5
UniProt: A0EL75
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase ges-5	protein	265	48% helix, 19% strand	A0EL75
B	Beta-lactamase ges-5	protein	265	49% helix, 19% strand	A0EL75

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B

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

Pockets

7 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	514	0.73	0.81	47	empty
2	106	0.46	0.79	18	empty
3	89	0.46	0.81	18	empty
4	64	0.39	0.80	24	empty
5	57	0.33	0.78	20	empty

Interfaces

1 interface between chains.

A–B · 913 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4GNU · Crystal structure of GES-5 carbapenemase · 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 A0EL75
Elsewhere: RCSB PDB 4GNU · PDBe 4GNU · UniProt A0EL75

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