Research workbench
Structure of regulatory chain mutant H20A of asparate transcarbamoylase from E. COLI
Analyse Structure of regulatory chain mutant H20A of asparate transcarbamoylase from E.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QGF
- 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
- ZN
- Pockets
- 10 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Aspartate carbamoyltransferase catalytic chain (EC 2.1.3.2) | protein | 310 | 41% helix, 16% strand | P0A786 |
| B, D | Aspartate carbamoyltransferase regulatory chain | protein | 153 | 14% helix, 37% strand | P0A7F3 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 293 | 0.63 | 0.80 | 31 | empty |
| 2 | 317 | 0.62 | 0.79 | 30 | empty |
| 3 | 330 | 0.61 | 0.78 | 37 | empty |
| 4 | 165 | 0.60 | 0.83 | 23 | empty |
| 5 | 168 | 0.48 | 0.77 | 25 | empty |
Interfaces
4 interfaces between chains.
- B–D · 1150 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 705 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 652 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 161 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2QGF · Structure of regulatory chain mutant H20A of asparate transcarbamoylase from E. coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0A7F3 · AlphaFold monomer V2.0 prediction for aspartate carbamoyltransferase regulatory chain… · a predicted model of the same protein · chain B against A, TM-score 0.92
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 2QGF · PDBe 2QGF · UniProt P0A786 · UniProt P0A7F3
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