MolNFT v1 · #141887 · protein
Nucleotide-free form of C. reinhardtii ARSA1
5ZME · ATPase ARSA1: “Nucleotide-free form of C. reinhardtii ARSA1”. X-ray diffraction, 1 ligand (PO4), 9 pockets (best druggability 0.83). MolNFT v1 #141887 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5ZME
- Type
- protein
- Length
- 638 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATPase ARSA1
- EC
- 3.6.-.-
- UniProt
- A8JGB0
- Ligands
- PO4
- Pockets
- 9 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATPase ARSA1 (EC 3.6.-.-) | protein | 638 | 48% helix, 14% strand | A8JGB0 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 973 | 0.83 | 0.84 | 105 | PO4 |
| 2 | 732 | 0.80 | 0.83 | 62 | empty |
| 3 | 307 | 0.64 | 0.80 | 36 | empty |
| 4 | 58 | 0.51 | 0.86 | 14 | empty |
| 5 | 115 | 0.44 | 0.77 | 15 | empty |
Modifications
Observed in the structure: 13 modified (engineered).
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 5ZME · PDBe 5ZME · UniProt A8JGB0
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