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PIN1 ww domain in complex with a phosphorylated CPEB1 derived peptide

Analyse PIN1 ww domain in complex with a phosphorylated CPEB1 derived peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2N1O
Type: protein
Length: 41 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase nima-interacting 1; Cytoplasmic polyadenylation…
EC: 5.2.1.8
UniProt: Q13526, Q9BZB8

Structure

solution nmr · 2 distinct chains · 0% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8)	protein	33	0% helix, 42% strand	Q13526
B	Cytoplasmic polyadenylation element-binding protein 1	protein	8	0% helix, 0% strand	Q9BZB8

Interfaces

1 interface between chains.

A–B · 349 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

2N1O · PIN1 WW domain in complex with a phosphorylated CPEB1 derived peptide · the same entry in another collection · chain A against A, TM-score 1.00
Q9BZB8 · AlphaFold monomer V2.0 prediction for cytoplasmic polyadenylation element-binding protein… · a predicted model of the same protein · chain B against A, TM-score 0.39

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 Q13526
Every structure of UniProt Q9BZB8
Elsewhere: RCSB PDB 2N1O · PDBe 2N1O · UniProt Q13526 · UniProt Q9BZB8

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