Research workbench
Emre multidrug transporter, apo crystal form
Analyse Emre multidrug transporter, apo crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B61
- Type
- protein
- Length
- 856 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multidrug transporter emre
- UniProt
- P23895
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Multidrug transporter emre | protein | 107 | 0% helix, 0% strand | P23895 |
Interfaces
6 interfaces between chains.
- E–F · 29 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 27 Ų buried · 0 hydrogen bonds · protein-protein
- G–H · 24 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 18 Ų buried · 0 hydrogen bonds · protein-protein
- E–G · 13 Ų buried · 0 hydrogen bonds · protein-protein
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 P23895
- Elsewhere: RCSB PDB 3B61 · PDBe 3B61 · UniProt P23895
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