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Crystal structure of class C beta-lactamase act-1

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

PDB: 2ZC7
Type: protein
Length: 1,436 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase act-1
EC: 3.5.2.6
UniProt: Q48428
Pockets: 11 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Beta-lactamase act-1 (EC 3.5.2.6)	protein	359	39% helix, 22% strand	Q48428

Pockets

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	570	0.70	0.79	70	empty
2	305	0.66	0.82	42	empty
3	337	0.66	0.81	48	empty
4	321	0.65	0.81	50	empty
5	298	0.54	0.75	38	empty

Interfaces

3 interfaces between chains.

C–D · 282 Å² buried · 3 hydrogen bonds · protein-protein
B–D · 230 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 203 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2ZC7 · Crystal Structure of Class C beta-Lactamase ACT-1 · 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 Q48428
Elsewhere: RCSB PDB 2ZC7 · PDBe 2ZC7 · UniProt Q48428

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