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2WFJ

Atomic resolution crystal structure of the PPIase domain of human cyclophilin G in complex with cyclosporin A.

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 Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1184
ChainResidue
ALYS48
AILE90
ATYR91
ASER99
AHOH2060
AHOH2180

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1185
ChainResidue
AHOH2172
AHOH2207
AHOH2209
AHOH2071
AHOH2074
AHOH2078

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1186
ChainResidue
AHOH2026
AHOH2039
AHOH2041
AHOH2103
AHOH2104
AHOH2246

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 1187
ChainResidue
AGLY86
AARG115
AGLY121
ASER122
AGLN123

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR CHAIN B OF CYCLOSPORIN A
ChainResidue
ATHR45
AGLY46
AGLU47
AGLY49
ATHR50
AARG67
APHE72
AGLN75
AGLY84
AALA113
AASN114
AARG115
AGLN123
APHE125
AHIS133
AHIS138
AHOH2136
BHOH2001
BHOH2003
BHOH2006
BHOH2007
BHOH2008
BHOH2009

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

218853

PDB entries from 2024-04-24

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