Research workbench
Structure of MHP1, a nucleobase-cation-symport-1 family transporter, in a closed conformation with indolylmethyl-hydantoin
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
- 4D1A
- Type
- protein
- Length
- 456 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydantoin transport protein
- UniProt
- D6R8X8
- Ligands
- I5H, NA
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydantoin transport protein | protein | 456 | 74% helix, 1% strand | D6R8X8 |
Ligands and binding sites
- I5H · (5S)-5-(1H-indol-3-ylmethyl)imidazolidine-2,4-dione · ligand · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.78 | 0.98 | 24 | I5H |
| 2 | 90 | 0.60 | 0.87 | 17 | empty |
| 3 | 125 | 0.47 | 0.78 | 22 | empty |
| 4 | 94 | 0.40 | 0.77 | 23 | empty |
| 5 | 94 | 0.35 | 0.74 | 18 | empty |
Compared structures
- 4D1A · 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 4D1A · PDBe 4D1A · UniProt D6R8X8
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