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1YAT

IMPROVED CALCINEURIN INHIBITION BY YEAST FKBP12-DRUG COMPLEXES. CRYSTALLOGRAPHIC AND FUNCTIONAL ANALYSIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0001228molecular_functionDNA-binding transcription activator activity, RNA polymerase II-specific
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005515molecular_functionprotein binding
A0005527molecular_functionmacrolide binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0006325biological_processchromatin organization
A0006366biological_processtranscription by RNA polymerase II
A0006457biological_processprotein folding
A0044183molecular_functionprotein folding chaperone
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0070651biological_processnonfunctional rRNA decay
A1901710biological_processregulation of homoserine biosynthetic process
A1903644biological_processregulation of chaperone-mediated protein folding
Functional Information from PDB Data
site_id506
Number of Residues12
Details
ChainResidue
ATYR26
AILE91
ATYR82
APHE99
APHE36
AASP37
APHE46
AGLN54
AVAL55
AILE56
ATRP59
APHE87

site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FK5 A 108
ChainResidue
ATYR26
APHE36
AASP37
AARG42
APHE46
AGLN54
AVAL55
AILE56
ATRP59
AALA81
ATYR82
APRO88
AILE91

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378
ChainResidueDetails
ASER-5

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER44

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
AILE56
ATYR82
AASP37

222926

PDB entries from 2024-07-24

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