MolNFT v1 · #57965 · protein
Crystal structure of the central axis (ntpd-ntpg) in the catalytic portion of enterococcus hirae V-type sodium ATPase
3AON · V-type sodium ATPase subunit D: “Crystal structure of the central axis (ntpd-ntpg) in the catalytic portion of enterococcus hirae V-type…”. X-ray diffraction, 1 ligand (NO3), 1 pocket (best druggability 0.55). MolNFT v1 #57965 on…
- PDB
- 3AON
- Type
- protein
- Length
- 289 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- V-type sodium ATPase subunit D; V-type sodium ATPase subunit G
- EC
- 3.6.3.14
- UniProt
- P43455
- Ligands
- NO3
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type sodium ATPase subunit D (EC 3.6.3.14) | protein | 188 | 74% helix, 10% strand | — |
| B | V-type sodium ATPase subunit G (EC 3.6.3.14) | protein | 101 | 48% helix, 24% strand | P43455 |
Ligands and binding sites
- NO3 · Nitrate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.55 | 0.86 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 2172 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 3AON · Crystal structure of the central axis (NtpD-NtpG) in the catalytic portion of… · the same entry in another collection · chain A against A, TM-score 1.00
- P43455 · AlphaFold monomer V2.0 prediction for V-type sodium ATPase subunit G (P43455) · a predicted model of the same protein · chain B against A, TM-score 0.92
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 P43455
- Elsewhere: RCSB PDB 3AON · PDBe 3AON · UniProt P43455
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