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Structural consequences of effector binding to the T state of aspartate carbamoyltransferase. crystal structures of the unligated and ATP-, and CTP-complexed enzymes at 2.6-ångströms resolution
Analyse Structural consequences of effector binding to the T state of aspartate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AT1
- Type
- protein
- Length
- 912 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate carbamoyltransferase (T state), catalytic chain; Aspartate carbamoyltransferase…
- EC
- 2.1.3.2
- UniProt
- P0A786, P0A7F3
- Ligands
- CTP, ZN
- Pockets
- 6 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Aspartate carbamoyltransferase (T state), catalytic chain (EC 2.1.3.2) | protein | 310 | 38% helix, 16% strand | P0A786 |
| B, D | Aspartate carbamoyltransferase regulatory chain | protein | 146 | 14% helix, 32% strand | P0A7F3 |
Ligands and binding sites
- 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
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 273 | 0.59 | 0.79 | 31 | empty |
| 2 | 300 | 0.58 | 0.78 | 29 | empty |
| 3 | 203 | 0.54 | 0.78 | 24 | empty |
| 4 | 177 | 0.48 | 0.77 | 33 | empty |
| 5 | 140 | 0.41 | 0.74 | 22 | empty |
Interfaces
3 interfaces between chains.
- B–D · 927 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 714 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 686 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 5AT1 · Structural consequences of effector binding to the T state of aspartate… · 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
- Every structure of UniProt P0A7F3
- Elsewhere: RCSB PDB 5AT1 · PDBe 5AT1 · UniProt P0A786 · UniProt P0A7F3
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