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Class C beta-lactamase from escherichia COLI

Analyse Class C beta-lactamase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XG1
Type: protein
Length: 720 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q104Z6
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	359	40% helix, 23% strand	Q104Z6
B	Beta-lactamase (EC 3.5.2.6)	protein	361	40% helix, 24% strand	Q104Z6

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 7 copies · chains A, B

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

Pockets

6 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	838	0.75	0.79	96	EDO
2	320	0.66	0.81	48	empty
3	144	0.44	0.76	28	empty
4	79	0.34	0.75	14	empty
5	80	0.31	0.73	18	empty

Interfaces

1 interface between chains.

A–B · 356 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6XG1 · Class C beta-lactamase from Escherichia coli · 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 Q104Z6
Elsewhere: RCSB PDB 6XG1 · PDBe 6XG1 · UniProt Q104Z6

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