2QDP

Crystal structure of the HePTP catalytic domain C270S mutant crystallized in ammonium acetate

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 PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 A 436

Chain	Residue
A	SER270
A	HOH466
A	HOH512
A	SER271
A	ALA272
A	GLY273
A	ILE274
A	GLY275
A	ARG276
A	GLN314
A	GLU335

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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, ECO:0000269|PubMed:9624114

Chain	Residue	Details
A	SER270

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING:

Chain	Residue	Details
A	ASP236
A	SER270
A	GLN314

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:10206983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR45

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:10206983

Chain	Residue	Details
A	SER72

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

Chain	Residue	Details
A	SER89

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER122

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000250

Chain	Residue	Details
A	SER270

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