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Crystal structure of the mono-zinc carbapenemase cpha from aeromonas hydrophyla

Analyse Crystal structure of the mono-zinc carbapenemase cpha from aeromonas hydrophyla in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1X8G
Type: protein
Length: 224 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: P26918
Ligands: ZN, CO3, SO4
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	224	30% helix, 25% strand	P26918

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CO3 · Carbonate ion · ion · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	257	0.63	0.81	25	CO3

Compared structures

1X8G · Crystal Structure of the Mono-Zinc Carbapenemase CphA from Aeromonas Hydrophyla · the same entry in another collection · chain A against A, TM-score 1.00
P26918 · AlphaFold monomer V2.0 prediction for metallo-beta-lactamase type 2 (P26918) · a predicted model of the same protein · 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 P26918
Elsewhere: RCSB PDB 1X8G · PDBe 1X8G · UniProt P26918

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