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Crystal structure of aspartate transcarbamoylase from trypanosoma cruzi in complex with aspartate (asp) and phosphate (pi).
Analyse Crystal structure of aspartate transcarbamoylase from trypanosoma cruzi in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JL5
- Type
- protein
- Length
- 1,899 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate carbamoyltransferase
- EC
- 2.1.3.2
- UniProt
- O15636
- Ligands
- ASP, PO4
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 6 distinct chains · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate carbamoyltransferase (EC 2.1.3.2) | protein | 317 | 47% helix, 15% strand | O15636 |
| B | Aspartate carbamoyltransferase (EC 2.1.3.2) | protein | 327 | 45% helix, 15% strand | O15636 |
| C | Aspartate carbamoyltransferase (EC 2.1.3.2) | protein | 306 | 44% helix, 15% strand | O15636 |
| D | Aspartate carbamoyltransferase (EC 2.1.3.2) | protein | 311 | 46% helix, 15% strand | O15636 |
| E | Aspartate carbamoyltransferase (EC 2.1.3.2) | protein | 314 | 45% helix, 15% strand | O15636 |
| F | Aspartate carbamoyltransferase (EC 2.1.3.2) | protein | 324 | 47% helix, 15% strand | O15636 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · 6 copies · chains A, B, C, D, E, F
- PO4 · Phosphate ion · ion · 6 copies · chains A, B, C, D, E, F
- GOL · Glycerol · additive · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 414 | 0.81 | 0.89 | 59 | empty |
| 2 | 347 | 0.81 | 0.91 | 47 | empty |
| 3 | 214 | 0.77 | 0.91 | 34 | empty |
| 4 | 72 | 0.73 | 0.97 | 24 | empty |
| 5 | 69 | 0.73 | 0.98 | 23 | PO4, ASP |
Interfaces
10 interfaces between chains.
- B–C · 1284 Ų buried · 19 hydrogen bonds · protein-protein
- D–E · 1281 Ų buried · 19 hydrogen bonds · protein-protein
- E–F · 1269 Ų buried · 22 hydrogen bonds · protein-protein
- D–F · 1252 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1251 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 6JL5 · Crystal structure of aspartate transcarbamoylase from Trypanosoma cruzi in complex with… · 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 O15636
- Elsewhere: RCSB PDB 6JL5 · PDBe 6JL5 · UniProt O15636
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