MolNFT v1 · #46749 · protein
Msreca-ATP-gama-S complex
2ODW · Protein reca: “Msreca-ATP-gama-S complex”. X-ray diffraction, 1 ligand (AGS), 4 pockets (best druggability 0.49). MolNFT v1 #46749 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2ODW
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein reca
- EC
- 3.4.99.37
- UniProt
- Q59560
- Ligands
- AGS
- Pockets
- 4 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein reca (EC 3.4.99.37) | protein | 308 | 35% helix, 24% strand | Q59560 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.49 | 0.77 | 25 | AGS |
| 2 | 135 | 0.42 | 0.75 | 24 | empty |
| 3 | 151 | 0.42 | 0.74 | 29 | empty |
| 4 | 52 | 0.26 | 0.74 | 14 | 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 Q59560
- Elsewhere: RCSB PDB 2ODW · PDBe 2ODW · UniProt Q59560
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