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Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases

Analyse Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ERZ
Type
protein
Length
606 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-carbamyl-D-amino acid amidohydrolase
EC
3.5.1.77
UniProt
P60327
Pockets
4 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BN-carbamyl-D-amino acid amidohydrolase (EC 3.5.1.77)protein30332% helix, 28% strandP60327

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12420.790.9239empty
22800.780.9043empty
3520.370.8014empty
4990.340.7422empty

Interfaces

1 interface between chains.

  • A–B · 2525 Ų buried · 24 hydrogen bonds · protein-protein

Compared structures

  • 1ERZ · Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic… · the same entry in another collection · chain A against A, TM-score 1.00
  • P60327 · AlphaFold monomer V2.0 prediction for N-carbamoyl-D-amino acid hydrolase (P60327) · a predicted model of the same protein · chain B against A, TM-score 1.00

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