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Ornithine transcarbamylase from escherichia COLI

Analyse Ornithine transcarbamylase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1AKM
Type
protein
Length
966 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ornithine transcarbamylase
EC
2.1.3.3
UniProt
P04391
Pockets
3 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, COrnithine transcarbamylase (EC 2.1.3.3)protein32247% helix, 15% strandP04391

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111220.880.89159empty
2550.310.7714empty
3780.310.7419empty

Interfaces

3 interfaces between chains.

  • A–B · 1113 Ų buried · 20 hydrogen bonds · protein-protein
  • B–C · 1089 Ų buried · 18 hydrogen bonds · protein-protein
  • A–C · 1078 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 1AKM · Ornithine transcarbamylase from escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00
  • P04391 · AlphaFold monomer V2.0 prediction for ornithine carbamoyltransferase subunit I (P04391) · a predicted model of the same protein · chain A against A, TM-score 0.99

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