Research workbench
NAVAB1P (bicelles)
Analyse NAVAB1P (bicelles) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PGI
- Type
- protein
- Length
- 1,170 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q0VNY2
- Ligands
- NA, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, F, G, H | — | protein | 146 | — | Q0VNY2 |
| D, E | — | protein | 147 | — | Q0VNY2 |
Ligands and binding sites
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D, E, F, G, H
- MG · Magnesium ion · metal · chains E, H
- ACT · Acetate ion · additive · 6 copies · chains B, C, D, E, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7PGI · NaVAb1p (bicelles) · 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 Q0VNY2
- Elsewhere: RCSB PDB 7PGI · PDBe 7PGI · UniProt Q0VNY2
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