MolNFT v1 · #23247 · protein
Aspartate transcarbamoylase catalytic chain mutant E50A complex with phosphonoacetamide, malonate, and cytidine-5-prime-triphosphate (CTP)
1TUG · Aspartate carbamoyltransferase catalytic chain: “Aspartate transcarbamoylase catalytic chain mutant E50A complex with phosphonoacetamide, malonate, and…”. X-ray diffraction, 3 ligands (PCT, CTP, ZN), 12 pockets (best druggability…
- PDB
- 1TUG
- Type
- protein
- Length
- 926 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate carbamoyltransferase catalytic chain; Aspartate carbamoyltransferase regulatory…
- EC
- 2.1.3.2
- UniProt
- P0A786, P0A7F3
- Ligands
- PCT, CTP, ZN
- Pockets
- 12 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Aspartate carbamoyltransferase catalytic chain (EC 2.1.3.2) | protein | 310 | 40% helix, 16% strand | P0A786 |
| B, D | Aspartate carbamoyltransferase regulatory chain | protein | 153 | 14% helix, 31% strand | P0A7F3 |
Ligands and binding sites
- PCT · Phosphonoacetamide · ligand · 2 copies · chains A, C
- CTP · Cytidine-5'-triphosphate · ligand · 2 copies · chains B, D
- ZN · Zinc ion · metal · 2 copies · chains B, C, D
- MLI · Malonate ion · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.62 | 0.93 | 17 | empty |
| 2 | 283 | 0.60 | 0.79 | 29 | MLI, PCT |
| 3 | 152 | 0.59 | 0.83 | 24 | empty |
| 4 | 199 | 0.50 | 0.76 | 24 | empty |
| 5 | 152 | 0.50 | 0.79 | 24 | PCT |
Interfaces
3 interfaces between chains.
- B–D · 1113 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 672 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 658 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1TUG · Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A786 · AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.98
- P0A7F3 · AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase regulatory chain… · a predicted model of the same protein · chain B against A, TM-score 0.91
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 P0A786
- Every structure of UniProt P0A7F3
- Elsewhere: RCSB PDB 1TUG · PDBe 1TUG · UniProt P0A786 · UniProt P0A7F3
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