Research workbench
Copper transporter OprC
Analyse Copper transporter OprC in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FOK
- Type
- protein
- Length
- 1,288 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.97
- Source
- Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847…
- Molecule
- Putative copper transport outer membrane porin OprC
- UniProt
- G3XD89
- Ligands
- CU
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · resolution 1.97 · 2 distinct chains · 4% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative copper transport outer membrane porin OprC | protein | 651 | 4% helix, 58% strand | G3XD89 |
| B | Putative copper transport outer membrane porin OprC | protein | 637 | 4% helix, 60% strand | G3XD89 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A, B
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 12 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 283 | 0.85 | 0.96 | 49 | empty |
| 2 | 281 | 0.85 | 0.96 | 42 | empty |
| 3 | 261 | 0.84 | 0.96 | 44 | empty |
| 4 | 165 | 0.80 | 0.96 | 44 | empty |
| 5 | 1192 | 0.80 | 0.82 | 104 | empty |
Interfaces
1 interface between chains.
- A–B · 602 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6FOK · Copper transporter oprc · the same entry in another collection · chain A against A, TM-score 1.00
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 G3XD89
- Elsewhere: RCSB PDB 6FOK · PDBe 6FOK · UniProt G3XD89
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