2RUC

Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity

Functional Information from PROSITE/UniProt

site_id	PS01096
Number of Residues	21
Details	PPIC_PPIASE_1 PpiC-type peptidyl-prolyl cis-trans isomerase signature. FEsLAsqfSdcs.Saka..RGdLG

Chain	Residue	Details
A	PHE57-GLY77

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	111
Details	Domain: {"description":"PpiC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00278","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by DAPK1","evidences":[{"source":"PubMed","id":"21497122","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29686383","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 511

Chain	Residue	Details
A	HIS13	proton shuttle (general acid/base)
A	CYS67	covalently attached, electrostatic stabiliser
A	GLN85	electrostatic stabiliser
A	SER108	electrostatic stabiliser
A	HIS111	electrostatic stabiliser

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