5HDE

Crystal Structure of PTPN12 Catalytic Domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004725	molecular_function	protein tyrosine phosphatase activity
A	0004726	molecular_function	non-membrane spanning protein tyrosine phosphatase activity
A	0006470	biological_process	protein dephosphorylation
A	0016311	biological_process	dephosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue PO4 A 401

Chain	Residue
A	CSP231
A	HOH563
A	HOH598
A	SER232
A	ALA233
A	GLY234
A	CYS235
A	GLY236
A	ARG237
A	THR238
A	GLN278

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE229-GLY239

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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	CSP231

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:27134172

Chain	Residue	Details
A	ARG36
A	ARG63
A	ASP199
A	GLN278

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	CSP231

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378

Chain	Residue	Details
A	MET1

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:27134172, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER19

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