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5EX2

Crystal structure of cyclophilin AquaCyp293 from Hirschia baltica

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0006457biological_processprotein folding
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0006457biological_processprotein folding
B0016853molecular_functionisomerase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 301
ChainResidue
AGLN113
AGLN131
AGLU133
AHOH410
AHOH710
AHOH769

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 302
ChainResidue
AGLY69
AARG173
AHOH886

site_idAC3
Number of Residues6
Detailsbinding site for residue CA B 301
ChainResidue
BGLN113
BGLN131
BGLU133
BHOH486
BHOH674
BHOH788

site_idAC4
Number of Residues2
Detailsbinding site for residue CL B 302
ChainResidue
BARG83
BASP86

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

220760

PDB entries from 2024-06-05

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