MolNFT v1 · #162484 · protein
Heterodimeric ABC exporter tmrab in vanadate trapped outward-facing occluded conformation
6RAK: “Heterodimeric ABC exporter tmrab in vanadate trapped outward-facing occluded conformation”. Electron microscopy, 3 ligands (AOV, ATP, MG). MolNFT v1 #162484 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6RAK
- Type
- protein
- Length
- 1,280 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q72J05, Q72J04
- Ligands
- AOV, ATP, MG
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 588 | — | Q72J05 |
| B | — | protein | 571 | — | Q72J04 |
| C | — | protein | 121 | — | — |
Ligands and binding sites
- AOV · Adp orthovanadate · ligand · chains A, B
- ATP · Adenosine-5'-triphosphate · ligand · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6RAK · Heterodimeric ABC exporter TmrAB in vanadate trapped outward-facing occluded conformation · 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 Q72J05
- Every structure of UniProt Q72J04
- Elsewhere: RCSB PDB 6RAK · PDBe 6RAK · UniProt Q72J05 · UniProt Q72J04
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