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4TW8

The Fk1-Fk2 domains of FKBP52 in complex with iFit-FL

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 37M A 301
ChainResidue
ATYR57
ALYS121
AARG189
AGLY59
AASP68
AGLY84
AGLU85
AVAL86
AILE87
ATRP90
ATYR113

site_idAC2
Number of Residues9
Detailsbinding site for residue 37M B 301
ChainResidue
BTYR57
BGLY59
BASP68
BGLY84
BGLU85
BVAL86
BILE87
BTRP90
BTYR113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues176
DetailsDomain: {"description":"PPIase FKBP-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues172
DetailsDomain: {"description":"PPIase FKBP-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by CK2","evidences":[{"source":"UniProtKB","id":"P27124","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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