MolNFT v1 · #172893 · protein
Opua inhibited inward facing
7AHE: “Opua inhibited inward facing”. Electron microscopy, 1 ligand (2BA). MolNFT v1 #172893 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7AHE
- Type
- protein
- Length
- 1,308 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0V8ETW8, A0A0R2NIU5
- Ligands
- 2BA
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 272 | — | A0A0V8ETW8 |
| C, D | — | protein | 382 | — | A0A0R2NIU5 |
Ligands and binding sites
- 2BA · (2r,3r,3as,5r,7ar,9r,10r,10as,12r,14ar)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-D:3', 2'-J][1,3,7,9,2,8 ]tetraoxadiphosphacyclododecine-3,5, 10,12-tetrol 5,12-dioxide · ligand · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7AHE · OpuA inhibited inward facing · 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 A0A0V8ETW8
- Every structure of UniProt A0A0R2NIU5
- Elsewhere: RCSB PDB 7AHE · PDBe 7AHE · UniProt A0A0V8ETW8 · UniProt A0A0R2NIU5
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