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Crystal structure of the PEPP1 pleckstrin homology domain in complex with inositol 1,3,4,5-tetrakisphosphate
Analyse Crystal structure of the PEPP1 pleckstrin homology domain in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UPR
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pleckstrin homology domain-containing family a member 4
- UniProt
- Q9H4M7
- Ligands
- 4IP
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pleckstrin homology domain-containing family a member 4 | protein | 107 | 17% helix, 36% strand | Q9H4M7 |
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.
Compared structures
- 1UPR · Crystal structure of the PEPP1 pleckstrin homology domain in complex with Inositol… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H4M7 · AlphaFold monomer V2.0 prediction for pleckstrin homology domain- containing family a… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9H4M7
- Elsewhere: RCSB PDB 1UPR · PDBe 1UPR · UniProt Q9H4M7
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