Research workbench
HSPEPT1 bound to ala-phe in the outward facing occluded conformation
Analyse HSPEPT1 bound to ala-phe in the outward facing occluded conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PMW
- Type
- protein
- Length
- 643 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P46059
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 641 | — | P46059 |
| B | — | protein | 2 | — | — |
Compared structures
- 7PMW · HsPepT1 bound to Ala-Phe in the outward facing occluded conformation · the same entry in another collection · chain A against A, TM-score 1.00
- P46059 · AlphaFold monomer V2.0 prediction for solute carrier family 15 member 1 (P46059) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P46059
- Elsewhere: RCSB PDB 7PMW · PDBe 7PMW · UniProt P46059
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