3ZFX

Crystal structure of EphB1

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
E	0004672	molecular_function	protein kinase activity
E	0004713	molecular_function	protein tyrosine kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0004713	molecular_function	protein tyrosine kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0004672	molecular_function	protein kinase activity
G	0004713	molecular_function	protein tyrosine kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004672	molecular_function	protein kinase activity
H	0004713	molecular_function	protein tyrosine kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation
I	0004672	molecular_function	protein kinase activity
I	0004713	molecular_function	protein tyrosine kinase activity
I	0005524	molecular_function	ATP binding
I	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 1890

Chain	Residue
A	ARG726
A	ALA730
A	LYS733

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	27
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGEFGEVYkGrlklpgkreiy.......VAIK

Chain	Residue	Details
A	ILE625-LYS651

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

Chain	Residue	Details
A	TYR740-VAL752

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP744
B	ASP744
C	ASP744
D	ASP744
E	ASP744
F	ASP744
G	ASP744
H	ASP744
I	ASP744

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site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE625
B	ILE625
C	ILE625
D	ILE625
E	ILE625
F	ILE625
G	ILE625
H	ILE625
I	ILE625

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site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LYS651
B	LYS651
C	LYS651
D	LYS651
E	LYS651
F	LYS651
G	LYS651
H	LYS651
I	LYS651

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