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Ges-1 beta-lactamase

Analyse Ges-1 beta-lactamase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QPN
Type: protein
Length: 531 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase ges-1
UniProt: Q9KJY7
Ligands: SO4
Pockets: 7 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase ges-1	protein	265	48% helix, 19% strand	Q9KJY7
B	Beta-lactamase ges-1	protein	266	49% helix, 19% strand	Q9KJY7

Ligands and binding sites

SO4 · Sulfate ion · ion · 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	517	0.72	0.80	46	empty
2	124	0.48	0.79	15	empty
3	81	0.46	0.81	17	empty
4	98	0.39	0.77	20	SO4
5	73	0.38	0.78	24	empty

Interfaces

1 interface between chains.

A–B · 907 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2QPN · GES-1 beta-lactamase · 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 Q9KJY7
Elsewhere: RCSB PDB 2QPN · PDBe 2QPN · UniProt Q9KJY7

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