Research workbench
Catalytic trimer of escherichia COLI aspartate transcarbamoylase
Analyse Catalytic trimer of escherichia COLI aspartate transcarbamoylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CSU
- Type
- protein
- Length
- 880 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (aspartate carbamoyltransferase)
- EC
- 2.1.3.2
- UniProt
- P0A786
- Ligands
- CA
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (aspartate carbamoyltransferase) (EC 2.1.3.2) | protein | 288 | 41% helix, 16% strand | P0A786 |
| B | Protein (aspartate carbamoyltransferase) (EC 2.1.3.2) | protein | 288 | 41% helix, 17% strand | P0A786 |
| C | Protein (aspartate carbamoyltransferase) (EC 2.1.3.2) | protein | 304 | 43% helix, 15% strand | P0A786 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 887 | 0.86 | 0.88 | 101 | empty |
| 2 | 290 | 0.70 | 0.85 | 46 | empty |
| 3 | 389 | 0.62 | 0.77 | 55 | empty |
| 4 | 272 | 0.58 | 0.79 | 41 | empty |
Interfaces
3 interfaces between chains.
- B–C · 996 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 920 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 810 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 3CSU · Catalytic trimer of escherichia COLI aspartate transcarbamoylase · 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 P0A786
- Elsewhere: RCSB PDB 3CSU · PDBe 3CSU · UniProt P0A786
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