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3ICH

Crystal structure of cyclophilin B at 1.2 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003723molecular_functionRNA binding
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005515molecular_functionprotein binding
A0005518molecular_functioncollagen binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005790cellular_componentsmooth endoplasmic reticulum
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006457biological_processprotein folding
A0016018molecular_functioncyclosporin A binding
A0016020cellular_componentmembrane
A0030593biological_processneutrophil chemotaxis
A0032991cellular_componentprotein-containing complex
A0034663cellular_componentendoplasmic reticulum chaperone complex
A0040018biological_processpositive regulation of multicellular organism growth
A0042470cellular_componentmelanosome
A0043231cellular_componentintracellular membrane-bounded organelle
A0044794biological_processpositive regulation by host of viral process
A0044829biological_processpositive regulation by host of viral genome replication
A0048471cellular_componentperinuclear region of cytoplasm
A0050821biological_processprotein stabilization
A0051082molecular_functionunfolded protein binding
A0060348biological_processbone development
A0061077biological_processchaperone-mediated protein folding
A0070062cellular_componentextracellular exosome
A0070063molecular_functionRNA polymerase binding
A1901873biological_processregulation of post-translational protein modification
Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YknSkFHRVIkdFMiQGG
ChainResidueDetails
ATYR56-GLY73

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS52

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS133

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ACYS170

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24369
ChainResidueDetails
ALYS177

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN116

222926

PDB entries from 2024-07-24

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