Research workbench
Ovine B0,+AT-rbat heterodimer
Analyse Ovine B0,+AT-rbat heterodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NF6
- Type
- protein
- Length
- 1,078 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A6P3EL78, A0A6P7DVK7
- Ligands
- CLR, LBN, NAG, CA
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 455 | — | A0A6P3EL78 |
| A | — | protein | 623 | — | A0A6P7DVK7 |
Ligands and binding sites
- CLR · Cholesterol · ligand · 2 copies · chains B, A
- LBN · 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine · ligand · chains B, A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NF6 · Ovine b0,+AT-rBAT heterodimer · the same entry in another collection · chain B against B, 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 A0A6P3EL78
- Every structure of UniProt A0A6P7DVK7
- Elsewhere: RCSB PDB 7NF6 · PDBe 7NF6 · UniProt A0A6P3EL78 · UniProt A0A6P7DVK7
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