Research workbench
High resolution helical reconstruction of the bacterial P-type ATPase copper transporter copa
Analyse High resolution helical reconstruction of the bacterial P-type ATPase copper… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J09
- Type
- protein
- Length
- 1,446 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper-exporting P-type ATPase a
- EC
- 3.6.3.-
- UniProt
- O29777
- Pockets
- 17 · best druggability 0.86
Structure
electron microscopy · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Copper-exporting P-type ATPase a (EC 3.6.3.-) | protein | 723 | 41% helix, 17% strand | O29777 |
Pockets
17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1042 | 0.86 | 0.87 | 117 | empty |
| 2 | 1081 | 0.86 | 0.87 | 120 | empty |
| 3 | 940 | 0.85 | 0.86 | 118 | empty |
| 4 | 1122 | 0.83 | 0.84 | 138 | empty |
| 5 | 500 | 0.77 | 0.85 | 60 | empty |
Interfaces
1 interface between chains.
- A–B · 676 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3J09 · High resolution helical reconstruction of the bacterial p-type ATPase copper transporter… · the same entry in another collection · chain B against B, TM-score 1.00
- O29777 · AlphaFold monomer V2.0 prediction for probable copper-exporting P-type ATPase (O29777) · a predicted model of the same protein · chain A against A, TM-score 0.50
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 O29777
- Elsewhere: RCSB PDB 3J09 · PDBe 3J09 · UniProt O29777
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