5HEZ

JAK2 kinase (JH1 domain) mutant P1057A in complex with TG101209

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004713	molecular_function	protein tyrosine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue CL A 1201

Chain	Residue
A	LYS1083
C	1M31202

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 1202

Chain	Residue
A	HIS886
A	HIS891
D	HIS886
D	HIS891

---

site_id	AC3
Number of Residues	10
Details	binding site for residue 1M3 A 1203

Chain	Residue
A	LEU1026
A	TRP1038
A	GLY1086
A	ARG1087
C	MET1064
C	LEU1082
C	LYS1083
A	PHE1019
A	TRP1020
A	TYR1021

---

site_id	AC4
Number of Residues	11
Details	binding site for residue 1M3 A 1204

Chain	Residue
A	LEU855
A	VAL863
A	ALA880
A	GLU930
A	LEU932
A	GLY935
A	ARG980
A	ASN981
A	LEU983
A	ASP994
B	ARG847

---

site_id	AC5
Number of Residues	2
Details	binding site for residue CL B 1201

Chain	Residue
B	LYS1083
D	1M31202

---

site_id	AC6
Number of Residues	11
Details	binding site for residue 1M3 B 1202

Chain	Residue
B	PHE1019
B	TRP1020
B	TYR1021
B	LEU1026
B	TRP1038
B	LEU1078
B	LEU1081
B	GLY1086
D	LEU1082
D	LYS1083
D	CL1201

---

site_id	AC7
Number of Residues	12
Details	binding site for residue 1M3 B 1203

Chain	Residue
A	ARG847
B	LEU855
B	GLY856
B	LYS857
B	VAL863
B	ALA880
B	GLU930
B	LEU932
B	GLY935
B	ARG980
B	LEU983
B	ASP994

---

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN B 1204

Chain	Residue
B	HIS886
B	HIS891
C	HIS886
C	HIS891

---

site_id	AC9
Number of Residues	14
Details	binding site for residue 1M3 C 1201

Chain	Residue
C	LEU855
C	GLY856
C	GLY858
C	VAL863
C	ALA880
C	MET929
C	GLU930
C	LEU932
C	GLY935
C	ARG980
C	LEU983
C	ASP994
C	HOH1308
D	ARG847

---

site_id	AD1
Number of Residues	10
Details	binding site for residue 1M3 C 1202

Chain	Residue
A	MET1064
A	ILE1079
A	LEU1082
A	CL1201
C	PHE1019
C	TRP1020
C	TYR1021
C	TRP1038
C	LEU1081
C	GLY1086

---

site_id	AD2
Number of Residues	2
Details	binding site for residue CL D 1201

Chain	Residue
B	1M31202
D	LYS1083

---

site_id	AD3
Number of Residues	11
Details	binding site for residue 1M3 D 1202

Chain	Residue
B	MET1064
B	LEU1082
B	CL1201
D	PHE1019
D	TRP1020
D	TYR1021
D	PRO1023
D	TRP1038
D	LEU1078
D	LEU1081
D	GLY1086

---

site_id	AD4
Number of Residues	11
Details	binding site for residue 1M3 D 1203

Chain	Residue
D	LEU932
D	GLY935
D	ASN981
D	LEU983
D	ASP994
C	ARG847
D	LEU855
D	GLY856
D	VAL863
D	ALA880
D	GLU930

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVEmCrydplqdntgevv.....AVKK

Chain	Residue	Details
A	LEU855-LYS883

---

site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLATRNILV

Chain	Residue	Details
A	TYR972-VAL984

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP976
B	ASP976
C	ASP976
D	ASP976

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU855
A	LYS882
B	LEU855
B	LYS882
C	LEU855
C	LYS882
D	LEU855
D	LYS882

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q62120

Chain	Residue	Details
A	TYR868
D	TYR868
D	TYR966
D	TYR972
A	TYR966
A	TYR972
B	TYR868
B	TYR966
B	TYR972
C	TYR868
C	TYR966
C	TYR972

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16174768

Chain	Residue	Details
A	PTR1007
B	PTR1007
C	PTR1007
D	PTR1007

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:16174768

Chain	Residue	Details
A	PTR1008
B	PTR1008
C	PTR1008
D	PTR1008

---