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AlphaFold monomer V2.0 prediction for zinc D-ala-D-ala carboxypeptidase (P00733)

Analyse AlphaFold monomer V2.0 prediction for zinc D-ala-D-ala carboxypeptidase (P00733) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P00733
Type
protein
Length
255 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xF3dC0C0AfbCaFe21EC13288d7b1F1aD875Dd78F1
Molecule
Zinc D-ala-D-ala carboxypeptidase
UniProt
P00733
Pockets
2 · best druggability 0.32

Structure

1 distinct chain · 30% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AZinc D-ala-D-ala carboxypeptidaseprotein25530% helix, 9% strandP00733

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1580.320.7617empty
2750.310.7419empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 1LBU · Hydrolase metallo (zn) dd-peptidase · an experimental structure of the same protein · chain A against A, TM-score 0.83
  • 1LBU · Hydrolase metallo (zn) dd-peptidase · an experimental structure of the same protein · chain A against A, TM-score 0.83

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