MolNFT v1 · #184426 · protein
RAB27A fusion with SLP2A-RBDA1 effector covalent adduct with CB1 in C123
7OPR: “RAB27A fusion with SLP2A-RBDA1 effector covalent adduct with CB1 in C123”. X-ray diffraction, 3 ligands (GNP, 05Y, MG). MolNFT v1 #184426 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7OPR
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9HCH5, P51159
- Ligands
- GNP, 05Y, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 218 | — | Q9HCH5, P51159 |
| B | — | protein | 208 | — | Q9HCH5, P51159 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · 2 copies · chains A, B
- 05Y · ~{N}-[1-(2-pyridin-2-ylethyl)benzimidazol-2-yl]propanamide · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- GOL · Glycerol · additive · 9 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7OPR · Rab27a fusion with Slp2a-RBDa1 effector covalent adduct with CB1 in C123 · the same entry in another collection · chain A against A, TM-score 1.00
- P51159 · AlphaFold monomer V2.0 prediction for RAS-related protein rab-27A (P51159) · a predicted model of the same protein · chain B against A, TM-score 0.85
- Q9HCH5 · AlphaFold monomer V2.0 prediction for synaptotagmin-like protein 2 (Q9HCH5) · a predicted model of the same protein · chain A against A, TM-score 0.28
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 Q9HCH5
- Every structure of UniProt P51159
- Elsewhere: RCSB PDB 7OPR · PDBe 7OPR · UniProt Q9HCH5 · UniProt P51159
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