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Solution structure of PIN1 ww domain complexed with CDC25 phosphothreonine peptide

Analyse Solution structure of PIN1 ww domain complexed with CDC25 phosphothreonine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1I8G
Type: protein
Length: 49 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: M-phase inducer phosphatase 3; Peptidyl-prolyl cis-trans isomerase nima-interacting 1
EC: 3.1.3.48, 5.2.1.8
UniProt: P30311, Q13526

Structure

solution nmr · 2 distinct chains · 0% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	M-phase inducer phosphatase 3 (EC 3.1.3.48)	protein	10	0% helix, 0% strand	P30311
B	Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8)	protein	39	0% helix, 33% strand	Q13526

Interfaces

1 interface between chains.

A–B · 295 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

1I8G · Solution structure of PIN1 ww domain complexed with CDC25 phosphothreonine peptide · the same entry in another collection · chain A against A, TM-score 1.00
P30311 · AlphaFold monomer V2.0 prediction for M-phase inducer phosphatase 3 (P30311) · a predicted model of the same protein · chain A against A, TM-score 0.34

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 P30311
Every structure of UniProt Q13526
Elsewhere: RCSB PDB 1I8G · PDBe 1I8G · UniProt P30311 · UniProt Q13526

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