2NLK

Crystal structure of D1 and D2 catalytic domains of human Protein Tyrosine Phosphatase Gamma (D1+D2 PTPRG)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004725	molecular_function	protein tyrosine phosphatase activity
A	0006470	biological_process	protein dephosphorylation
A	0016311	biological_process	dephosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00383
Number of Residues	11
Details	TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGvgRTG

Chain	Residue	Details
A	VAL1058-GLY1068

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044

Chain	Residue	Details
A	ASN975

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASN943
A	ASN975
A	ILE1019

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Ancestral active site

Chain	Residue	Details
A	ARG1266

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692

Chain	Residue	Details
A	THR1097

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1ytw

Chain	Residue	Details
A	GLU955
A	CYS1060
A	ASP1028
A	THR1067
A	HIS1059
A	ARG1066

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site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1ytw

Chain	Residue	Details
A	ASP1028
A	CYS1060
A	THR1067
A	ARG1066

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