3MX0

Crystal Structure of EphA2 ectodomain in complex with ephrin-A5

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	0016020	cellular_component	membrane
B	0046875	molecular_function	ephrin receptor binding
B	0048013	biological_process	ephrin receptor signaling pathway
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	0016020	cellular_component	membrane
D	0046875	molecular_function	ephrin receptor binding
D	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. FqDiGACVALLSVRVyykKCP

Chain	Residue	Details
A	PHE182-PRO202

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site_id	PS00791
Number of Residues	21
Details	RECEPTOR_TYR_KIN_V_2 Receptor tyrosine kinase class V signature 2. CavDGEWlv.PIGqClCqaGYE

Chain	Residue	Details
A	CYS247-GLU267

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site_id	PS01186
Number of Residues	14
Details	EGF_2 EGF-like domain signature 2. ClCqaGYekveda..C

Chain	Residue	Details
A	CYS260-CYS273

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

Chain	Residue	Details
B	LYS113-SER140

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17400922

Chain	Residue	Details
B	ASN37
D	ASN37

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site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218

Chain	Residue	Details
A	ASN435
C	ASN435

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