Structure of PDB 1yat Chain A

Receptor sequence

>1yatA (length=113) Species: 4932 (Saccharomyces cerevisiae)

SEVIEGNVKIDRISPGDGATFPKTGDLVTIHYTGTLENGQKFDSSVDRGS
PFQCNIGVGQVIKGWDVGIPKLSVGEKARLTIPGPYAYGPRGFPGLIPPN
STLVFDVELLKVN

3D structure

• PDB: 1yat Improved calcineurin inhibition by yeast FKBP12-drug complexes. Crystallographic and functional analysis.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y26 F36 D37 I56 Y82 F99
• Catalytic site (residue number reindexed from 1): Y32 F42 D43 I62 Y88 F105
• Enzyme Commision number: 5.2.1.8: peptidylprolyl isomerase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FK5	A	Y26 D37 F46 V55 I56 W59 Y82	Y32 D43 F52 V61 I62 W65 Y88

Gene Ontology

Molecular Function

• GO:0001228 DNA-binding transcription activator activity, RNA polymerase II-specific
• GO:0003755 peptidyl-prolyl cis-trans isomerase activity
• GO:0005515 protein binding
• GO:0005527 macrolide binding
• GO:0044183 protein folding chaperone

Biological Process

• GO:0006325 chromatin organization
• GO:0006366 transcription by RNA polymerase II
• GO:0006457 protein folding
• GO:0045944 positive regulation of transcription by RNA polymerase II
• GO:0070651 nonfunctional rRNA decay
• GO:1901710 regulation of homoserine biosynthetic process
• GO:1903644 regulation of chaperone-mediated protein folding

Cellular Component

• GO:0005634 nucleus
• GO:0005737 cytoplasm
• GO:0005739 mitochondrion

External links

• PDB: RCSB:1yat, PDBe:1yat, PDBj:1yat
• PDBsum: 1yat
• PubMed: 7681823
• UniProt: P20081|FKBP_YEAST FK506-binding protein 1 (Gene Name=FPR1)