6FNH

Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with a pyrazolo[3,4-d]pyrimidine fragment of NVP-BHG712

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue DXK A 1001

Chain	Residue
A	ILE619
A	HOH1274
A	ALA621
A	ALA644
A	THR692
A	GLU693
A	MET695
A	LEU746
A	EDO1006
A	HOH1212

---

site_id	AC2
Number of Residues	3
Details	binding site for residue EDO A 1002

Chain	Residue
A	GLN852
A	ARG860
A	PRO862

---

site_id	AC3
Number of Residues	2
Details	binding site for residue EDO A 1003

Chain	Residue
A	GLN669
A	HOH1109

---

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO A 1004

Chain	Residue
A	TYR735
A	VAL736
A	HIS737
A	HOH1215

---

site_id	AC5
Number of Residues	6
Details	binding site for residue EDO A 1005

Chain	Residue
A	TYR791
A	LYS793
A	HOH1158
A	HOH1208
C	ASP708
C	EDO1003

---

site_id	AC6
Number of Residues	4
Details	binding site for residue EDO A 1006

Chain	Residue
A	ARG743
A	ASN744
A	ASP757
A	DXK1001

---

site_id	AC7
Number of Residues	2
Details	binding site for residue EDO A 1007

Chain	Residue
A	ASP888
C	EDO1002

---

site_id	AC8
Number of Residues	1
Details	binding site for residue EDO A 1008

Chain	Residue
A	GLN669

---

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO A 1009

Chain	Residue
A	THR795
A	ARG858
A	HOH1180
C	GLU706

---

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 1010

Chain	Residue
A	LEU714
A	GLY718
A	HOH1166
A	HOH1173

---

site_id	AD2
Number of Residues	4
Details	binding site for residue EDO A 1011

Chain	Residue
A	ASP708
A	THR812
A	GLU815
A	HOH1138

---

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO A 1012

Chain	Residue
A	ASN750
A	HOH1225
A	HOH1335
B	GLN616
B	LYS617
B	TYR628

---

site_id	AD4
Number of Residues	9
Details	binding site for residue DXK B 1001

Chain	Residue
B	ILE619
B	ALA621
B	ALA644
B	THR692
B	GLU693
B	MET695
B	LEU746
B	HOH1189
B	HOH1250

---

site_id	AD5
Number of Residues	1
Details	binding site for residue EDO B 1002

Chain	Residue
B	ASN750

---

site_id	AD6
Number of Residues	2
Details	binding site for residue EDO B 1003

Chain	Residue
B	ALA770
B	ILE779

---

site_id	AD7
Number of Residues	5
Details	binding site for residue EDO B 1004

Chain	Residue
A	HOH1202
B	LYS684
B	TYR685
B	EDO1005
B	HOH1111

---

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO B 1005

Chain	Residue
B	TYR685
B	EDO1004
B	HOH1229

---

site_id	AD9
Number of Residues	8
Details	binding site for residue DXK C 1001

Chain	Residue
C	ALA621
C	GLY622
C	ALA644
C	THR692
C	GLU693
C	MET695
C	LEU746
C	HOH1134

---

site_id	AE1
Number of Residues	5
Details	binding site for residue EDO C 1002

Chain	Residue
A	ASP888
A	EDO1007
C	GLN852
C	ARG860
C	PRO862

---

site_id	AE2
Number of Residues	3
Details	binding site for residue EDO C 1003

Chain	Residue
A	EDO1005
C	ASP708
C	GLY709

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE619-LYS646

---

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

Chain	Residue	Details
A	TYR735-VAL747

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	27
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q03145","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---