1PXH

Crystal structure of protein tyrosine phosphatase 1B with potent and selective bidentate inhibitor compound 2

Replaces:  1N6W

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	5
Details	BINDING SITE FOR RESIDUE MG A 322

Chain	Residue
A	HOH605
A	HOH606
A	HOH607
A	HOH608
A	HOH609

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 323

Chain	Residue
A	HOH529
A	HOH540
A	HOH542

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site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SNA A 401

Chain	Residue
A	LYS41
A	TYR46
A	ARG47
A	ASP48
A	ASP181
A	PHE182
A	CYS215
A	SER216
A	ALA217
A	GLY218
A	ILE219
A	GLY220
A	ARG221
A	GLN262
A	HOH570
A	HOH604
A	LYS5

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY A 402

Chain	Residue
A	ARG79
A	SER205
A	HOH517
A	HOH528

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site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY A 403

Chain	Residue
A	GLU76
A	LEU234
A	LYS248
A	HOH566

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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. VHCsaGigRSG

Chain	Residue	Details
A	VAL213-GLY223

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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	CYS215

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	ASP181

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

Chain	Residue	Details
A	CYS215
A	GLN262

---

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

Chain	Residue	Details
A	MET1

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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	TYR20

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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	SER50

---

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

Chain	Residue	Details
A	TYR66

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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	CYS215

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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	SER242
A	SER243

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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	CYS215
A	SER216

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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	ARG221
A	ASP181
A	CYS215
A	SER222

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 469

Chain	Residue	Details
A	ASP181	proton shuttle (general acid/base)
A	CYS215	covalent catalysis
A	ARG221	activator, electrostatic stabiliser
A	SER222	activator, electrostatic stabiliser
A	GLN262	steric role

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