Research workbench
Crystal structure of E. COLI argininosuccinate synthetase in complex with ATP and citrulline
Analyse Crystal structure of E. COLI argininosuccinate synthetase in complex with ATP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KP3
- Type
- protein
- Length
- 439 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Argininosuccinate synthetase
- EC
- 6.3.4.5
- UniProt
- P0A6E4
- Ligands
- CIR, GAI, ATP, PO4
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Argininosuccinate synthetase (EC 6.3.4.5) | protein | 439 | 41% helix, 18% strand | P0A6E4 |
Ligands and binding sites
- CIR · Citrulline · ligand · 2 copies · chains A
- GAI · Guanidine · ligand · 2 copies · chains A
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 856 | 0.75 | 0.79 | 74 | ATP, CIR |
| 2 | 66 | 0.37 | 0.78 | 17 | empty |
| 3 | 54 | 0.25 | 0.72 | 16 | empty |
Compared structures
- 1KP3 · Crystal Structure of E. coli Argininosuccinate Synthetase in Complex with ATP and… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6E4 · AlphaFold monomer V2.0 prediction for argininosuccinate synthase (P0A6E4) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P0A6E4
- Elsewhere: RCSB PDB 1KP3 · PDBe 1KP3 · UniProt P0A6E4
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