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2GW2

Crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin G

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0006457biological_processprotein folding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX A 1001
ChainResidue
AARG152

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX A 1002
ChainResidue
AHIS59
ATYR60
ALYS61
ACYS63
APHE79

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 1003
ChainResidue
AALA113
AASN114
AHIS138

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 1004
ChainResidue
AGLU38
ALYS48
AHOH210

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YksClFHRVVkdFMvQGG
ChainResidueDetails
ATYR60-GLY77

222926

PDB entries from 2024-07-24

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