4DIP

Crystal structure of human Peptidyl-prolyl cis-trans isomerase FKBP14

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
B	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
C	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
D	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
E	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
F	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
G	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
H	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
I	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
J	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE NA B 201

Chain	Residue
B	ASN136

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 G 201

Chain	Residue
D	GLN73
D	HOH267
G	ARG40
G	ARG135
G	ASN136

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	900
Details	Domain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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