MolNFT v1 · #136263 · protein
Critical role of water molecules for proton translocation of the membrane-bound transhydrogenase
5UNI: “Critical role of water molecules for proton translocation of the membrane-bound transhydrogenase”. X-ray diffraction, 1 ligand (BEN). MolNFT v1 #136263 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UNI
- Type
- protein
- Length
- 355 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q72GR9, Q72GS0
- Ligands
- BEN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 94 | — | Q72GR9 |
| B | — | protein | 261 | — | Q72GS0 |
Ligands and binding sites
- BEN · Benzamidine · ligand · 3 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 7 copies · chains A, B
- 1PE · Pentaethylene glycol · additive · 4 copies · chains A, B
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UNI · Critical role of water molecules for proton translocation of the membrane-bound… · the same entry in another collection · chain A against A, 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 Q72GR9
- Every structure of UniProt Q72GS0
- Elsewhere: RCSB PDB 5UNI · PDBe 5UNI · UniProt Q72GR9 · UniProt Q72GS0
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