Research workbench
Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline
Analyse Crystal structure of human argininosuccinate synthase in complex with aspartate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NZ2
- Type
- protein
- Length
- 402 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Argininosuccinate synthase
- EC
- 6.3.4.5
- UniProt
- P00966
- Ligands
- ASP, CIR, NA
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Argininosuccinate synthase (EC 6.3.4.5) | protein | 402 | 44% helix, 20% strand | P00966 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · chains A
- CIR · Citrulline · ligand · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 963 | 0.75 | 0.78 | 68 | ASP, CIR |
Compared structures
- 2NZ2 · Crystal structure of human argininosuccinate synthase in complex with aspartate and… · the same entry in another collection · chain A against A, TM-score 1.00
- P00966 · AlphaFold monomer V2.0 prediction for argininosuccinate synthase (P00966) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00966
- Elsewhere: RCSB PDB 2NZ2 · PDBe 2NZ2 · UniProt P00966
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