3C1N

Crystal Structure of Allosteric Inhibition Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-threonine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004072	molecular_function	aspartate kinase activity
A	0005829	cellular_component	cytosol
A	0008652	biological_process	amino acid biosynthetic process
A	0009088	biological_process	L-threonine biosynthetic process
A	0009089	biological_process	obsolete L-lysine biosynthetic process via diaminopimelate
A	0009090	biological_process	L-homoserine biosynthetic process
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
B	0004072	molecular_function	aspartate kinase activity
B	0005829	cellular_component	cytosol
B	0008652	biological_process	amino acid biosynthetic process
B	0009088	biological_process	L-threonine biosynthetic process
B	0009089	biological_process	obsolete L-lysine biosynthetic process via diaminopimelate
B	0009090	biological_process	L-homoserine biosynthetic process
B	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
C	0004072	molecular_function	aspartate kinase activity
C	0005829	cellular_component	cytosol
C	0008652	biological_process	amino acid biosynthetic process
C	0009088	biological_process	L-threonine biosynthetic process
C	0009089	biological_process	obsolete L-lysine biosynthetic process via diaminopimelate
C	0009090	biological_process	L-homoserine biosynthetic process
C	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
D	0004072	molecular_function	aspartate kinase activity
D	0005829	cellular_component	cytosol
D	0008652	biological_process	amino acid biosynthetic process
D	0009088	biological_process	L-threonine biosynthetic process
D	0009089	biological_process	obsolete L-lysine biosynthetic process via diaminopimelate
D	0009090	biological_process	L-homoserine biosynthetic process
D	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE THR B 470

Chain	Residue
A	ASN434
A	ILE435
B	MET414
B	ALA417
B	LYS418
B	ILE420
B	ALA421
B	GLN440
B	GLU444

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE THR A 471

Chain	Residue
A	MET414
A	ALA417
A	GLY419
A	ILE420
A	ALA421
A	GLN440
A	GLU444
B	ASN434
B	ILE435

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE THR D 472

Chain	Residue
C	ASN434
C	ILE435
D	MET414
D	ALA417
D	LYS418
D	ILE420
D	ALA421
D	GLN440
D	GLU444

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE THR A 473

Chain	Residue
A	LYS6
A	GLY8
A	GLY9
A	THR10
A	SER11
A	TRP229
A	THR230
A	ASP231

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE THR B 474

Chain	Residue
B	LYS6
B	GLY8
B	GLY9
B	THR10
B	SER11
B	TRP229
B	THR230
B	ASP231

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE THR C 475

Chain	Residue
C	GLY8
C	THR10
C	SER11
C	TRP229
C	THR230
C	ASP231
C	LYS266

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE THR D 476

Chain	Residue
D	LYS6
D	GLY8
D	GLY9
D	THR10
D	SER11
D	TRP229
D	THR230
D	ASP231

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Functional Information from PROSITE/UniProt

site_id	PS00324
Number of Residues	9
Details	ASPARTOKINASE Aspartokinase signature. VmKFGGTSV

Chain	Residue	Details
A	VAL4-VAL12

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