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Crystal structure of beta-LACTAMASE/D-alanine carboxypeptidase from yersinia pestis

Analyse Crystal structure of beta-LACTAMASE/D-alanine carboxypeptidase from yersinia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OZH
Type
protein
Length
351 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-LACTAMASE/D-alanine carboxypeptidase
UniProt
Q7CHA2
Pockets
1 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-LACTAMASE/D-alanine carboxypeptidaseprotein35134% helix, 20% strandQ7CHA2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11840.530.7839empty

Modifications

Observed in the structure: 13 modified, 1 disulfide (engineered, disulfide).

Compared structures

  • 3OZH · Crystal Structure of Beta-Lactamase/D-alanine Carboxypeptidase from Yersinia pestis · the same entry in another collection · chain A against A, TM-score 1.00

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