1FWL

CRYSTAL STRUCTURE OF HOMOSERINE KINASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004413	molecular_function	homoserine kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006566	biological_process	threonine metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009088	biological_process	threonine biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
B	0000166	molecular_function	nucleotide binding
B	0004413	molecular_function	homoserine kinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006566	biological_process	threonine metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0009088	biological_process	threonine biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
C	0000166	molecular_function	nucleotide binding
C	0004413	molecular_function	homoserine kinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006566	biological_process	threonine metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0009088	biological_process	threonine biosynthetic process
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
D	0000166	molecular_function	nucleotide binding
D	0004413	molecular_function	homoserine kinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006566	biological_process	threonine metabolic process
D	0008652	biological_process	amino acid biosynthetic process
D	0009088	biological_process	threonine biosynthetic process
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity

Functional Information from PROSITE/UniProt

site_id	PS00627
Number of Residues	12
Details	GHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. VKaGsGLGSSAA

Chain	Residue	Details
A	VAL89-ALA100

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1fwk

Chain	Residue	Details
A	THR183

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1fwk

Chain	Residue	Details
B	THR183

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site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1fwk

Chain	Residue	Details
C	THR183

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site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1fwk

Chain	Residue	Details
D	THR183

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 778

Chain	Residue	Details
A	GLU130	metal ligand
A	THR183	electrostatic stabiliser, polar interaction

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site_id	MCSA2
Number of Residues	2
Details	M-CSA 778

Chain	Residue	Details
B	GLU130	metal ligand
B	THR183	electrostatic stabiliser, polar interaction

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site_id	MCSA3
Number of Residues	2
Details	M-CSA 778

Chain	Residue	Details
C	GLU130	metal ligand
C	THR183	electrostatic stabiliser, polar interaction

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site_id	MCSA4
Number of Residues	2
Details	M-CSA 778

Chain	Residue	Details
D	GLU130	metal ligand
D	THR183	electrostatic stabiliser, polar interaction

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