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Crystal structure of mgs domain of carbamoyl-phosphate synthetase from homo sapiens

Analyse Crystal structure of mgs domain of carbamoyl-phosphate synthetase from homo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YVQ
Type
protein
Length
134 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Carbamoyl-phosphate synthase
EC
6.3.4.16
UniProt
P31327
Pockets
2 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACarbamoyl-phosphate synthase (EC 6.3.4.16)protein13449% helix, 15% strandP31327

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1580.390.8026empty
2580.270.7316empty

Compared structures

  • 2YVQ · Crystal structure of MGS domain of carbamoyl-phosphate synthetase from homo sapiens · the same entry in another collection · chain A against A, TM-score 1.00
  • P31327 · AlphaFold monomer V2.0 prediction for carbamoyl-phosphate synthase [ammonia]… · a predicted model of the same protein · chain A against A, TM-score 0.89

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