Research workbench
The structure of wild-type E. COLI aspartate transcarbamoylase in complex with novel T state inhibitors at 2.50 resolution
Analyse The structure of wild-type E. COLI aspartate transcarbamoylase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FZK
- Type
- protein
- Length
- 924 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
- EOZ, CTP, ZN
- Pockets
- 8 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Aspartate carbamoyltransferase catalytic chain (EC 2.1.3.2) | protein | 310 | 39% helix, 16% strand | P0A786 |
| B, D | Aspartate carbamoyltransferase regulatory chain (EC 2.1.3.2) | protein | 152 | 13% helix, 24% strand | P0A7F3 |
Ligands and binding sites
- EOZ · 3,5-bis[(phosphonoacetyl)amino]benzoic acid · ligand · 2 copies · chains A, C
- CTP · Cytidine-5'-triphosphate · ligand · 2 copies · chains B, D
- 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
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.67 | 0.82 | 34 | CTP |
| 2 | 264 | 0.63 | 0.81 | 31 | EOZ |
| 3 | 227 | 0.58 | 0.80 | 32 | EOZ |
| 4 | 191 | 0.49 | 0.76 | 28 | empty |
| 5 | 140 | 0.48 | 0.78 | 26 | CTP |
Interfaces
3 interfaces between chains.
- B–D · 1091 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 681 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 652 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 2FZK · The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T… · 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 0.91
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 2FZK · PDBe 2FZK · UniProt P0A786 · UniProt P0A7F3
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