MolNFT v1 · #91070 · protein
The crystal structure of ornithine carbamoyltransferase from burkholderia thailandensis E264
4F2G · Ornithine carbamoyltransferase 1: “The crystal structure of ornithine carbamoyltransferase from burkholderia thailandensis E264”. X-ray diffraction, 1 ligand (PO4), 1 pocket (best druggability 0.46). MolNFT v1 #91070 on GenesisL1…
- PDB
- 4F2G
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ornithine carbamoyltransferase 1
- EC
- 2.1.3.3
- UniProt
- Q2T0L1
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ornithine carbamoyltransferase 1 (EC 2.1.3.3) | protein | 290 | 46% helix, 18% strand | Q2T0L1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.46 | 0.78 | 29 | PO4 |
Compared structures
- 4F2G · The Crystal Structure of Ornithine carbamoyltransferase from Burkholderia thailandensis… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q2T0L1
- Elsewhere: RCSB PDB 4F2G · PDBe 4F2G · UniProt Q2T0L1
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