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1Q1C

Crystal structure of N(1-260) of human FKBP52

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS A 301
ChainResidue
AVAL86
AILE87
ATRP90

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 302
ChainResidue
ALEU182
AHOH356

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE DMS A 303
ChainResidue
ATRP60

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 304
ChainResidue
AGLN209
AHOH503
AGLU166
AGLY193
ATYR202

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 305
ChainResidue
AGLY139
AARG153

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
ATYR161
ALYS163
AHOH401

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylmethionine; in peptidyl-prolyl cis-trans isomerase FKBP4; alternate => ECO:0000269|Ref.5
ChainResidueDetails
ATHR2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partial => ECO:0000269|Ref.5
ChainResidueDetails
AALA3

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CK2 => ECO:0000250|UniProtKB:P27124
ChainResidueDetails
AGLU144

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ALEU221

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
ATYR113
AASP68
AILE87

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
ALEU198
AASP184
APHE227

222036

PDB entries from 2024-07-03

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