1NMW

Solution structure of the PPIase domain of human Pin1

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 200

Chain	Residue
A	LYS63
A	ARG68
A	ARG69
A	SER154

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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	PHE103-GLY123

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphoserine; by DAPK1 => ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:29686383

Chain	Residue	Details
A	SER71

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332

Chain	Residue	Details
A	SER108

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 9200606

Chain	Residue	Details
A	CYS113
A	HIS59
A	HIS157

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 511

Chain	Residue	Details
A	HIS59	proton shuttle (general acid/base)
A	CYS113	covalently attached, electrostatic stabiliser
A	GLN131	electrostatic stabiliser
A	SER154	electrostatic stabiliser
A	HIS157	electrostatic stabiliser

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