4BBE

Aminoalkylpyrimidine Inhibitor Complexes with JAK2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein 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	11
Details	BINDING SITE FOR RESIDUE 3O4 A 2229

Chain	Residue
A	LEU855
A	ASP994
B	GLN853
A	PHE860
A	VAL863
A	LYS882
A	GLU930
A	TYR931
A	LEU932
A	GLY935
A	LEU983

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 3O4 B 2229

Chain	Residue
A	GLN853
B	LEU855
B	GLY856
B	VAL863
B	GLU930
B	TYR931
B	LEU932
B	GLY935
B	LYS943
B	LEU983

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 3O4 C 2229

Chain	Residue
C	LEU855
C	VAL863
C	LYS882
C	MET929
C	GLU930
C	TYR931
C	LEU932
C	GLY935
D	GLN853

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 3O4 D 2229

Chain	Residue
C	GLN853
D	LEU855
D	PHE860
D	VAL863
D	ALA880
D	LYS882
D	GLU930
D	TYR931
D	LEU932
D	GLY935
D	ASP939
D	LEU983
D	ASP994
D	HOH2009

---

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

---

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	ASN976
B	ASN976
C	ASN976
D	ASN976

---

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

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

---

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

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

---

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

Chain	Residue	Details
A	TYR1007
B	TYR1007
C	TYR1007
D	TYR1007

---

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

Chain	Residue	Details
A	TYR1008
B	TYR1008
C	TYR1008
D	TYR1008

---