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Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form

Analyse Structure of the catalytic chain of methanococcus jannaschii aspartate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4EKN
Type
protein
Length
304 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aspartate carbamoyltransferase
EC
2.1.3.2
UniProt
Q58976
Ligands
K, SO4
Pockets
2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BAspartate carbamoyltransferase (EC 2.1.3.2)protein30446% helix, 14% strandQ58976

Ligands and binding sites

  • K · Potassium ion · metal · chains B
  • SO4 · Sulfate ion · ion · 4 copies · chains B
  • GOL · Glycerol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12540.560.7838SO4
2670.360.7714empty

Compared structures

  • 4EKN · Structure of the catalytic chain of Methanococcus jannaschii Aspartate Transcarbamoylase… · the same entry in another collection · chain B against B, TM-score 1.00
  • Q58976 · AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase (Q58976) · a predicted model of the same protein · chain B against A, TM-score 0.95

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