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4JCP

Structure of Cyclophilin B from Brugia malayi

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 SO4 A 201
ChainResidue
AARG48
AGLY87
AGLU88
ALYS89
AHOH438
AHOH453

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
AHOH486
AHIS54
ALYS56
ALYS132

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 203
ChainResidue
AARG3
AGLU97
AARG138

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
ALYS31
ASER154
AGLN155
ASER156
AHOH347
AHOH397

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 205
ChainResidue
AASN94
APHE95

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgSkFHRVIpnFMlQGG
ChainResidueDetails
ATYR55-GLY72

225946

PDB entries from 2024-10-09

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