8F88

Crystal structure of PTP1B D181A/Q262A/C215A phosphatase domain with monophosphorylated JAK2 activation loop phosphopeptide

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
B	0004725	molecular_function	protein tyrosine phosphatase activity
B	0006470	biological_process	protein dephosphorylation
B	0016311	biological_process	dephosphorylation
C	0004725	molecular_function	protein tyrosine phosphatase activity
C	0006470	biological_process	protein dephosphorylation
C	0016311	biological_process	dephosphorylation

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16174768

Chain	Residue	Details
E	TYR1162
F	TYR1162
G	TYR1162

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:16174768

Chain	Residue	Details
E	PTR1163
F	PTR1163
G	PTR1163

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ALA215
A	ALA262
B	ALA215
B	ALA262
C	ALA215
C	ALA262

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2546149

Chain	Residue	Details
A	MET1
B	MET1
C	MET1

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455

Chain	Residue	Details
A	TYR20
B	TYR20
C	TYR20

---

site_id	SWS_FT_FI6
Number of Residues	3
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
B	SER50
C	SER50

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by EGFR => ECO:0000269|PubMed:9355745

Chain	Residue	Details
A	TYR66
B	TYR66
C	TYR66

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000269|PubMed:22169477

Chain	Residue	Details
A	ALA215
B	ALA215
C	ALA215

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	MOD_RES: Phosphoserine; by CLK1 and CLK2 => ECO:0000269|PubMed:10480872

Chain	Residue	Details
A	SER242
A	SER243
B	SER242
B	SER243
C	SER242
C	SER243

---

site_id	SWS_FT_FI10
Number of Residues	6
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	ALA215
A	SER216
B	ALA215
B	SER216
C	ALA215
C	SER216

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 469

Chain	Residue	Details
A	ALA181	proton shuttle (general acid/base)
A	ALA215	covalent catalysis
A	ARG221	activator, electrostatic stabiliser
A	SER222	activator, electrostatic stabiliser
A	ALA262	steric role

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 469

Chain	Residue	Details
B	ALA181	proton shuttle (general acid/base)
B	ALA215	covalent catalysis
B	ARG221	activator, electrostatic stabiliser
B	SER222	activator, electrostatic stabiliser
B	ALA262	steric role

---

site_id	MCSA3
Number of Residues	5
Details	M-CSA 469

Chain	Residue	Details
C	ALA181	proton shuttle (general acid/base)
C	ALA215	covalent catalysis
C	ARG221	activator, electrostatic stabiliser
C	SER222	activator, electrostatic stabiliser
C	ALA262	steric role

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