5EX1

Crystal structure of cyclophilin AquaCyp300 from Hirschia baltica

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000413	biological_process	protein peptidyl-prolyl isomerization
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
A	0046872	molecular_function	metal ion binding
B	0000413	biological_process	protein peptidyl-prolyl isomerization
B	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
B	0046872	molecular_function	metal ion binding
C	0000413	biological_process	protein peptidyl-prolyl isomerization
C	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
C	0046872	molecular_function	metal ion binding
D	0000413	biological_process	protein peptidyl-prolyl isomerization
D	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
D	0046872	molecular_function	metal ion binding
E	0000413	biological_process	protein peptidyl-prolyl isomerization
E	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
E	0046872	molecular_function	metal ion binding
F	0000413	biological_process	protein peptidyl-prolyl isomerization
F	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG B 301

Chain	Residue
B	ASP171
B	HOH435
B	HOH455
B	HOH584
D	ASP171
D	HOH430

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site_id	AC2
Number of Residues	6
Details	binding site for residue MG C 301

Chain	Residue
F	HOH384
F	HOH429
F	HOH458
C	ASP171
C	HOH572
F	ASP171

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site_id	AC3
Number of Residues	3
Details	binding site for residue MG E 301

Chain	Residue
E	ASP171
E	HOH524
E	HOH565

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