Research workbench
Amppnp complex of C. reinhardtii ARSA1
Analyse Amppnp complex of C. reinhardtii ARSA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZMF
- Type
- protein
- Length
- 637 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATPase ARSA1
- EC
- 3.6.-.-
- UniProt
- A8JGB0
- Ligands
- ANP, MG
- Pockets
- 5 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATPase ARSA1 (EC 3.6.-.-) | protein | 637 | 47% helix, 14% strand | A8JGB0 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1144 | 0.84 | 0.85 | 95 | empty |
| 2 | 1119 | 0.78 | 0.80 | 88 | ANP, MG |
| 3 | 249 | 0.63 | 0.81 | 26 | empty |
| 4 | 51 | 0.60 | 0.92 | 14 | empty |
| 5 | 63 | 0.45 | 0.83 | 16 | empty |
Compared structures
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 A8JGB0
- Elsewhere: RCSB PDB 5ZMF · PDBe 5ZMF · UniProt A8JGB0
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