Research workbench
Solution structure of PIN1 ww domain complexed with human tau phosphothreonine peptide
Analyse Solution structure of PIN1 ww domain complexed with human tau phosphothreonine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I8H
- Type
- protein
- Length
- 52 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-associated protein tau; Peptidyl-prolyl cis-trans isomerase nima-interacting 1
- EC
- 5.2.1.8
- UniProt
- P10636, Q13526
Structure
solution nmr · 2 distinct chains · 0% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Microtubule-associated protein tau | protein | 13 | 0% helix, 0% strand | P10636 |
| B | Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8) | protein | 39 | 0% helix, 21% strand | Q13526 |
Interfaces
1 interface between chains.
- A–B · 345 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 1I8H · Solution structure of PIN1 ww domain complexed with human tau phosphothreonine peptide · 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 P10636
- Every structure of UniProt Q13526
- Elsewhere: RCSB PDB 1I8H · PDBe 1I8H · UniProt P10636 · UniProt Q13526
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