3ZEP

Crystal Structure of JAK3 Kinase Domain in Complex with a Pyrrolopyrazine-2-phenyl Ether Inhibitor

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	13
Details	BINDING SITE FOR RESIDUE 1NX A 2099

Chain	Residue
A	LEU828
A	ASN954
A	LEU956
A	ASP967
A	HOH2025
A	GLY829
A	LYS830
A	VAL836
A	ALA853
A	GLU903
A	TYR904
A	LEU905
A	GLY908

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 1NX B 2101

Chain	Residue
B	GLN827
B	LEU828
B	ALA853
B	MET902
B	GLU903
B	TYR904
B	LEU905
B	GLY908
B	CYS909
B	ARG953
B	LEU956
B	HOH2030
C	ARG916

---

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 1NX C 2101

Chain	Residue
B	ARG916
C	GLN827
C	LEU828
C	VAL836
C	ALA853
C	MET902
C	GLU903
C	TYR904
C	LEU905
C	GLY908
C	CYS909
C	ASN954
C	LEU956
C	ASP967
C	HOH2023
C	HOH2073

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1NX D 2100

Chain	Residue
D	LEU828
D	GLY829
D	LYS830
D	VAL836
D	ALA853
D	GLU903
D	TYR904
D	LEU905
D	CYS909
D	ASN954
D	LEU956

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 2102

Chain	Residue
B	ARG920
C	GLU837

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGNFGSVElCrydplgdntgal......VAVK

Chain	Residue	Details
A	LEU828-LYS855

---

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

Chain	Residue	Details
A	CYS945-VAL957

---

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	ASP949
B	ASP949
C	ASP949
D	ASP949

---

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

Chain	Residue	Details
C	LEU828
C	LYS855
D	LEU828
D	LYS855
A	LEU828
A	LYS855
B	LEU828
B	LYS855

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:18250158

Chain	Residue	Details
C	TYR904
C	TYR939
D	TYR904
D	TYR939
A	TYR904
A	TYR939
B	TYR904
B	TYR939

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15831699

Chain	Residue	Details
C	PTR980
A	PTR980
A	PTR981
B	PTR980
B	PTR981
C	PTR981
D	PTR980
D	PTR981

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