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2IGV

CYCLOPHILIN 3 Complexed with DIPEPTIDE SER-PRO

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006457biological_processprotein folding
A0016018molecular_functioncyclosporin A binding
A0016853molecular_functionisomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SER A 201
ChainResidue
ALYS56
AHOH209
AHOH215
AHOH217
AALA108
AASN109
AHIS133
APRO202
AHOH204
AHOH205
AHOH206
AHOH207

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PRO A 202
ChainResidue
AARG62
APHE67
AGLN70
APHE120
AHIS133
ASER201
AHOH206
AHOH212

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. FkgSkFHRIIpnFMiQGG
ChainResidueDetails
APHE55-GLY72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues163
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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