Research workbench
Crystal structure of the ABC transporter in the cobalt transport system
Analyse Crystal structure of the ABC transporter in the cobalt transport system in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YZ2
- Type
- protein
- Length
- 529 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative ABC transporter ATP-binding protein TM_0222
- EC
- 3.6.3.-
- UniProt
- Q9WY65
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ABC transporter ATP-binding protein TM_0222 (EC 3.6.3.-) | protein | 266 | 35% helix, 23% strand | Q9WY65 |
| B | Putative ABC transporter ATP-binding protein TM_0222 (EC 3.6.3.-) | protein | 263 | 39% helix, 23% strand | Q9WY65 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 941 | 0.82 | 0.84 | 102 | empty |
| 2 | 119 | 0.60 | 0.85 | 20 | empty |
| 3 | 224 | 0.56 | 0.78 | 23 | empty |
| 4 | 196 | 0.50 | 0.76 | 28 | empty |
| 5 | 64 | 0.35 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1015 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2YZ2 · Crystal structure of the ABC transporter in the cobalt transport system · the same entry in another collection · chain A against A, TM-score 1.00
- Q9WY65 · AlphaFold monomer V2.0 prediction for energy-coupling factor transporter ATP-binding… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9WY65
- Elsewhere: RCSB PDB 2YZ2 · PDBe 2YZ2 · UniProt Q9WY65
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