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Crystal structure of the C-terminal deleted mutant of the class a carbapenemase kpc-2 at 1.23 ångström

Analyse Crystal structure of the C-terminal deleted mutant of the class a carbapenemase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3C5A
Type
protein
Length
264 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Class a carbapenemase kpc-2
UniProt
A8DS27
Pockets
1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AClass a carbapenemase kpc-2protein26444% helix, 17% strandA8DS27

Ligands and binding sites

  • CIT · Citric acid · additive · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1860.320.7419CIT

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3C5A · Crystal structure of the C-terminal deleted mutant of the class A carbapenemase KPC-2 at… · the same entry in another collection · chain A against A, TM-score 1.00

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