MolNFT v1 · #77194 · protein
Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis
3R7F · Aspartate carbamoyltransferase: “Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis”. X-ray diffraction, 2 ligands (CP, PO4), 7 pockets (best druggability 0.76). MolNFT v1 #77194 on GenesisL1: 3D…
- PDB
- 3R7F
- Type
- protein
- Length
- 873 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate carbamoyltransferase
- EC
- 2.1.3.2
- UniProt
- P05654
- Ligands
- CP, PO4
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Aspartate carbamoyltransferase (EC 2.1.3.2) | protein | 291 | 40% helix, 15% strand | P05654 |
Ligands and binding sites
- CP · Phosphoric acid mono(formamide)ester · ligand · 4 copies · chains A, B, C
- PO4 · Phosphate ion · ion · 13 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 683 | 0.76 | 0.82 | 61 | PO4 |
| 2 | 300 | 0.73 | 0.86 | 37 | CP |
| 3 | 489 | 0.70 | 0.80 | 45 | CP |
| 4 | 383 | 0.68 | 0.81 | 32 | CP |
| 5 | 59 | 0.30 | 0.75 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1050 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 964 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 951 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3R7F · Crystal Structure of CP-bound Aspartate Transcarbamoylase from Bacillus subtilis · the same entry in another collection · chain B against B, TM-score 1.00
- P05654 · AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase (P05654) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P05654
- Elsewhere: RCSB PDB 3R7F · PDBe 3R7F · UniProt P05654
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