Research workbench
Inward-facing conformation of the zinc transporter yiip revealed by cryo-electron microscopy
Analyse Inward-facing conformation of the zinc transporter yiip revealed by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J1Z
- Type
- protein
- Length
- 592 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cation efflux family protein
- UniProt
- Q8E919
- Pockets
- 8 · best druggability 0.76
Structure
electron microscopy · 1 distinct chain · 53% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P, Q | Cation efflux family protein | protein | 296 | 53% helix, 7% strand | Q8E919 |
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 465 | 0.76 | 0.84 | 61 | empty |
| 2 | 94 | 0.72 | 0.94 | 23 | empty |
| 3 | 319 | 0.66 | 0.81 | 43 | empty |
| 4 | 260 | 0.64 | 0.81 | 32 | empty |
| 5 | 237 | 0.61 | 0.81 | 27 | empty |
Interfaces
1 interface between chains.
- P–Q · 2830 Ų buried · 61 hydrogen bonds · protein-protein
Compared structures
- 3J1Z · Inward-Facing Conformation of the Zinc Transporter YiiP revealed by Cryo-electron… · the same entry in another collection · chain P against P, 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 Q8E919
- Elsewhere: RCSB PDB 3J1Z · PDBe 3J1Z · UniProt Q8E919
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