1PA1

Crystal structure of the C215D mutant of protein tyrosine phosphatase 1B

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	6
Details	BINDING SITE FOR RESIDUE MG A 4000

Chain	Residue
A	HOH4001
A	HOH4002
A	HOH4003
A	HOH4004
A	HOH4005
A	HOH4006

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 4010

Chain	Residue
A	HOH4014
A	HOH4015
A	HOH4016
A	HOH4011
A	HOH4012
A	HOH4013

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL A 5001

Chain	Residue
A	ARG545
A	PRO589
A	CYS621
A	ALA622
A	LYS739
A	HOH1086

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 5002

Chain	Residue
A	ARG612
A	VAL613
A	HIS675
A	HOH1084
A	HOH1242

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site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 5003

Chain	Residue
A	LYS616
A	GLY617
A	SER705
A	HOH1034

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site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 5004

Chain	Residue
A	ARG524
A	ARG754
A	GLN762

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site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 5005

Chain	Residue
A	ARG612
A	ASP681

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site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 5006

Chain	Residue
A	PRO538
A	LYS539

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Phosphocysteine intermediate

Chain	Residue	Details
A	ASP715

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	ASP681

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASP715
A	GLN762

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2546149

Chain	Residue	Details
A	MET501

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455

Chain	Residue	Details
A	TYR520

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKB/AKT1, CLK1 and CLK2 => ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:11579209, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER550

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745

Chain	Residue	Details
A	TYR566

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477

Chain	Residue	Details
A	ASP715

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site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872

Chain	Residue	Details
A	SER742
A	SER743

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site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form => ECO:0000269|PubMed:12802338, ECO:0000269|PubMed:12802339

Chain	Residue	Details
A	ASP715
A	SER716

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1bzc

Chain	Residue	Details
A	ARG721
A	SER722
A	ASP715
A	ASP681

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 469

Chain	Residue	Details
A	ASP681	proton shuttle (general acid/base)
A	ASP715	covalent catalysis
A	ARG721	activator, electrostatic stabiliser
A	SER722	activator, electrostatic stabiliser
A	GLN762	steric role

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