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3BKP

Crystal structure of the Toxoplasma gondii cyclophilin, 49.m03261

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 Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ASER19
AGLU41
AARG101
ALEU102
AHOH397

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AASN60
AHOH447

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AASN194
APRO201
AHOH354
AHOH398
ALEU54
AARG144

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
AHIS27
AASP86
ATHR87
AARG202
AARG203
AHOH343
AHOH368
AHOH382
AHOH444

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YvnTiFHRVVkdFIvQGG
ChainResidueDetails
ATYR58-GLY75

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PDB entries from 2024-07-10

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