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Crystal structure of the beta lactamase class D from chitinophaga pinensis by serial crystallography

Analyse Crystal structure of the beta lactamase class D from chitinophaga pinensis by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7K3M
Type
protein
Length
245 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-lactamase
EC
3.5.2.6
UniProt
C7PL61
Pockets
1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-lactamase (EC 3.5.2.6)protein24539% helix, 24% strandC7PL61

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11760.470.7521empty

Modifications

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

Compared structures

  • 7K3M · Crystal Structure of the Beta Lactamase Class D from Chitinophaga pinensis by Serial… · the same entry in another collection · chain A against A, TM-score 1.00

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