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AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP1B (P68106)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P68106
Type: protein
Length: 108 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x68C50954adA417a9303e7cEcfC2b256525160CC6
UniProt: P68106

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	108	—	P68106

Compared structures

4C02 · Crystal structure of human ACVR1 (ALK2) in complex with FKBP12.6 and dorsomorphin · an experimental structure of the same protein · chain A against B, TM-score 0.98
4C02 · Crystal structure of human ACVR1 (ALK2) in complex with FKBP12.6 and dorsomorphin · an experimental structure of the same protein · chain A against B, TM-score 0.98
7UA3 · Structure of PKA phosphorylated human RyR2-R2474S in the closed state in the presence of… · an experimental structure of the same protein · chain A against G, TM-score 0.98
7U9X · Structure of PKA phosphorylated human RyR2-R2474S in the closed state · an experimental structure of the same protein · chain A against G, TM-score 0.98
7UA4 · Structure of PKA phosphorylated human RyR2-R2474S in the open state in the presence of… · an experimental structure of the same protein · chain A against G, 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 P68106
Elsewhere: UniProt P68106 · AlphaFold DB P68106

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