Research workbench
Crystal structure of the O-carbamoyltransferase tobz M473I variant in complex with carbamoyl phosphate and ADP
Analyse Crystal structure of the O-carbamoyltransferase tobz M473I variant in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VF2
- Type
- protein
- Length
- 566 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- O-carbamoyltransferase tobz
- EC
- 2.1.3.-
- UniProt
- Q70IY1
- Ligands
- CP, ADP, FE2, K
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-carbamoyltransferase tobz (EC 2.1.3.-) | protein | 566 | 37% helix, 21% strand | Q70IY1 |
Ligands and binding sites
- CP · Phosphoric acid mono(formamide)ester · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- FE2 · Fe (II) ion · metal · chains A
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1095 | 0.83 | 0.84 | 106 | CP, ADP |
| 2 | 141 | 0.56 | 0.81 | 25 | empty |
| 3 | 61 | 0.32 | 0.76 | 14 | empty |
Compared structures
- 3VF2 · Crystal structure of the O-carbamoyltransferase TobZ M473I variant in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q70IY1 · AlphaFold monomer V2.0 prediction for nebramycin 5' synthase (Q70IY1) · a predicted model of the same protein · 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 Q70IY1
- Elsewhere: RCSB PDB 3VF2 · PDBe 3VF2 · UniProt Q70IY1
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