MolNFT v1 · #6577 · protein
GRP1 pH domain with INS(1,3,4,5)P4
1FGY: “GRP1 pH domain with INS(1,3,4,5)P4”. X-ray diffraction, 1 ligand (4IP), 1 pocket (best druggability 0.46). MolNFT v1 #6577 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1FGY
- Type
- protein
- Length
- 127 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GRP1
- UniProt
- O08967
- Ligands
- 4IP
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GRP1 | protein | 127 | 13% helix, 37% strand | O08967 |
Ligands and binding sites
- 4IP · Inositol-(1,3,4,5)-tetrakisphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.46 | 0.79 | 19 | 4IP |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
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 O08967
- Elsewhere: RCSB PDB 1FGY · PDBe 1FGY · UniProt O08967
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