Research workbench
Msreca-ADP-complex
Analyse Msreca-ADP-complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OEP
- Type
- protein
- Length
- 324 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
- ADP
- Pockets
- 6 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein reca (EC 3.4.99.37) | protein | 324 | 34% helix, 22% strand | Q59560 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.46 | 0.76 | 25 | ADP |
| 2 | 93 | 0.45 | 0.80 | 20 | empty |
| 3 | 174 | 0.43 | 0.74 | 33 | empty |
| 4 | 140 | 0.42 | 0.75 | 29 | empty |
| 5 | 51 | 0.28 | 0.75 | 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 Q59560
- Elsewhere: RCSB PDB 2OEP · PDBe 2OEP · UniProt Q59560
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