1KGY

Crystal Structure of the EphB2-ephrinB2 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005003	molecular_function	ephrin receptor activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
A	0016020	cellular_component	membrane
B	0005003	molecular_function	ephrin receptor activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
B	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
B	0016020	cellular_component	membrane
C	0005003	molecular_function	ephrin receptor activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
C	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
C	0016020	cellular_component	membrane
D	0005003	molecular_function	ephrin receptor activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
D	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
D	0016020	cellular_component	membrane
E	0016020	cellular_component	membrane
E	0046875	molecular_function	ephrin receptor binding
E	0048013	biological_process	ephrin receptor signaling pathway
F	0016020	cellular_component	membrane
F	0046875	molecular_function	ephrin receptor binding
F	0048013	biological_process	ephrin receptor signaling pathway
G	0016020	cellular_component	membrane
G	0046875	molecular_function	ephrin receptor binding
G	0048013	biological_process	ephrin receptor signaling pathway
H	0016020	cellular_component	membrane
H	0046875	molecular_function	ephrin receptor binding
H	0048013	biological_process	ephrin receptor signaling pathway

Functional Information from PROSITE/UniProt

site_id	PS00790
Number of Residues	21
Details	RECEPTOR_TYR_KIN_V_1 Receptor tyrosine kinase class V signature 1. FqDyGGCMSLIAVRVfyrKCP

Chain	Residue	Details
A	PHE186-PRO206

---

site_id	PS01299
Number of Residues	28
Details	EPHRIN_RBD_1 Ephrin receptor-binding (ephrin RBD) domain signature. KFTiKFQeFSPnlwGlEFqknkdYYiiS

Chain	Residue	Details
E	LYS1112-SER1139

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	544
Details	Domain: {"description":"Ephrin RBD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00884","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11703926","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---