Research workbench
Structure of MHP1, a nucleobase-cation-symport-1 family transporter, in a closed conformation with bromovinylhydantoin bound.
Analyse Structure of MHP1, a nucleobase-cation-symport-1 family transporter, in a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D1C
- Type
- protein
- Length
- 456 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D6R8X8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 456 | — | D6R8X8 |
Compared structures
- 4D1C · STRUCTURE OF MHP1, A NUCLEOBASE-CATION-SYMPORT-1 FAMILY TRANSPORTER, IN A CLOSED… · the same entry in another collection · chain A against A, TM-score 1.00
- D6R8X8 · AlphaFold monomer V2.0 prediction for hydantoin permease (D6R8X8) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 D6R8X8
- Elsewhere: RCSB PDB 4D1C · PDBe 4D1C · UniProt D6R8X8
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