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Association of subunit D (VMA6P) and E (VMA4P) with G (VMA10P) and the NMR solution structure of subunit G (G1-59) of the saccharomyces cerevisiae V1VO ATPase
Analyse Association of subunit D (VMA6P) and E (VMA4P) with G (VMA10P) and the NMR… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K88
- Type
- protein
- Length
- 60 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar proton pump subunit G
- EC
- 3.6.3.14
- UniProt
- P48836
Structure
solution nmr · 1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar proton pump subunit G (EC 3.6.3.14) | protein | 60 | 77% helix, 0% strand | P48836 |
Compared structures
- 2K88 · Association of subunit d (Vma6p) and E (Vma4p) with G (Vma10p) and the NMR solution… · the same entry in another collection · chain A against A, TM-score 1.00
- P48836 · AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit G (P48836) · a predicted model of the same protein · chain A against A, TM-score 0.74
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 P48836
- Elsewhere: RCSB PDB 2K88 · PDBe 2K88 · UniProt P48836
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