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Crystal structure of the class a extended-spectrum beta- lactamase per-2

Analyse Crystal structure of the class a extended-spectrum beta- lactamase per-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4D2O
Type
protein
Length
555 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Per-2 beta-lactamase
EC
3.5.2.6
UniProt
A2RP81
Pockets
3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APer-2 beta-lactamase (EC 3.5.2.6)protein27745% helix, 21% strandA2RP81
BPer-2 beta-lactamase (EC 3.5.2.6)protein27846% helix, 20% strandA2RP81

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18870.750.7988empty
22790.660.8236empty
32330.620.8133empty

Interfaces

1 interface between chains.

  • A–B · 1095 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 4D2O · Crystal structure of the class A extended-spectrum beta-lactamase PER- 2 · the same entry in another collection · chain A against A, TM-score 1.00

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