MolNFT v1 · #187122 · protein
Crystal structure of the NA+/H+ antiporter nhaa at pH 6.5
7S24 · NA(+)/H(+) antiporter nhaa: “Crystal structure of the NA+/H+ antiporter nhaa at pH 6.5”. X-ray diffraction, 7 pockets (best druggability 0.65). MolNFT v1 #187122 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7S24
- Type
- protein
- Length
- 375 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NA(+)/H(+) antiporter nhaa
- UniProt
- Q53YW7
- Pockets
- 7 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NA(+)/H(+) antiporter nhaa | protein | 375 | 75% helix, 2% strand | Q53YW7 |
Ligands and binding sites
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 2 copies · chains A
- 1PE · Pentaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.65 | 0.85 | 23 | empty |
| 2 | 136 | 0.53 | 0.81 | 22 | empty |
| 3 | 94 | 0.41 | 0.78 | 20 | empty |
| 4 | 81 | 0.41 | 0.78 | 14 | empty |
| 5 | 115 | 0.40 | 0.74 | 25 | empty |
Compared structures
- 7S24 · Crystal structure of the Na+/H+ antiporter NhaA at pH 6.5 · 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 Q53YW7
- Elsewhere: RCSB PDB 7S24 · PDBe 7S24 · UniProt Q53YW7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.