Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3AB4

Crystal structure of feedback inhibition resistant mutant of aspartate kinase from Corynebacterium glutamicum in complex with lysine and threonine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004072	molecular_function	aspartate kinase activity
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0008652	biological_process	amino acid biosynthetic process
A	0009085	biological_process	lysine biosynthetic process
A	0009088	biological_process	threonine biosynthetic process
A	0009089	biological_process	lysine biosynthetic process via diaminopimelate
A	0009090	biological_process	homoserine biosynthetic process
A	0016301	molecular_function	kinase activity
A	0019877	biological_process	diaminopimelate biosynthetic process
C	0004072	molecular_function	aspartate kinase activity
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0008652	biological_process	amino acid biosynthetic process
C	0009085	biological_process	lysine biosynthetic process
C	0009088	biological_process	threonine biosynthetic process
C	0009089	biological_process	lysine biosynthetic process via diaminopimelate
C	0009090	biological_process	homoserine biosynthetic process
C	0016301	molecular_function	kinase activity
C	0019877	biological_process	diaminopimelate biosynthetic process
E	0004072	molecular_function	aspartate kinase activity
E	0005524	molecular_function	ATP binding
E	0005829	cellular_component	cytosol
E	0008652	biological_process	amino acid biosynthetic process
E	0009085	biological_process	lysine biosynthetic process
E	0009088	biological_process	threonine biosynthetic process
E	0009089	biological_process	lysine biosynthetic process via diaminopimelate
E	0009090	biological_process	homoserine biosynthetic process
E	0016301	molecular_function	kinase activity
E	0019877	biological_process	diaminopimelate biosynthetic process
G	0004072	molecular_function	aspartate kinase activity
G	0005524	molecular_function	ATP binding
G	0005829	cellular_component	cytosol
G	0008652	biological_process	amino acid biosynthetic process
G	0009085	biological_process	lysine biosynthetic process
G	0009088	biological_process	threonine biosynthetic process
G	0009089	biological_process	lysine biosynthetic process via diaminopimelate
G	0009090	biological_process	homoserine biosynthetic process
G	0016301	molecular_function	kinase activity
G	0019877	biological_process	diaminopimelate biosynthetic process
I	0004072	molecular_function	aspartate kinase activity
I	0005524	molecular_function	ATP binding
I	0005829	cellular_component	cytosol
I	0008652	biological_process	amino acid biosynthetic process
I	0009085	biological_process	lysine biosynthetic process
I	0009088	biological_process	threonine biosynthetic process
I	0009089	biological_process	lysine biosynthetic process via diaminopimelate
I	0009090	biological_process	homoserine biosynthetic process
I	0016301	molecular_function	kinase activity
I	0019877	biological_process	diaminopimelate biosynthetic process
K	0004072	molecular_function	aspartate kinase activity
K	0005524	molecular_function	ATP binding
K	0005829	cellular_component	cytosol
K	0008652	biological_process	amino acid biosynthetic process
K	0009085	biological_process	lysine biosynthetic process
K	0009088	biological_process	threonine biosynthetic process
K	0009089	biological_process	lysine biosynthetic process via diaminopimelate
K	0009090	biological_process	homoserine biosynthetic process
K	0016301	molecular_function	kinase activity
K	0019877	biological_process	diaminopimelate biosynthetic process
M	0004072	molecular_function	aspartate kinase activity
M	0005524	molecular_function	ATP binding
M	0005829	cellular_component	cytosol
M	0008652	biological_process	amino acid biosynthetic process
M	0009085	biological_process	lysine biosynthetic process
M	0009088	biological_process	threonine biosynthetic process
M	0009089	biological_process	lysine biosynthetic process via diaminopimelate
M	0009090	biological_process	homoserine biosynthetic process
M	0016301	molecular_function	kinase activity
M	0019877	biological_process	diaminopimelate biosynthetic process
O	0004072	molecular_function	aspartate kinase activity
O	0005524	molecular_function	ATP binding
O	0005829	cellular_component	cytosol
O	0008652	biological_process	amino acid biosynthetic process
O	0009085	biological_process	lysine biosynthetic process
O	0009088	biological_process	threonine biosynthetic process
O	0009089	biological_process	lysine biosynthetic process via diaminopimelate
O	0009090	biological_process	homoserine biosynthetic process
O	0016301	molecular_function	kinase activity
O	0019877	biological_process	diaminopimelate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE THR A 501

Chain	Residue
A	ASP274
B	ASN125
B	ILE126
A	LYS275
A	GLY277
A	GLU278
A	ALA279
A	GLN298
A	THR308
A	HOH613
A	HOH622

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE LYS A 601

Chain	Residue
A	MET354
A	HIS357
A	PRO358
A	VAL360
A	THR361
A	SER381
A	GLU382
A	HOH610
A	HOH621
B	ASN43
B	ILE44
B	ASP45

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE THR B 201

Chain	Residue
A	ASN374
A	ILE375
B	ASP25
B	LYS26
B	GLY28
B	GLU29
B	ALA30
B	GLN49
B	HOH203

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE THR C 501

Chain	Residue
C	ASP274
C	LYS275
C	PRO276
C	GLY277
C	GLU278
C	ALA279
C	GLN298
C	THR308
C	HOH622
C	HOH623
D	ASN125
D	ILE126

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LYS C 601

Chain	Residue
C	MET354
C	HIS357
C	PRO358
C	VAL360
C	THR361
C	SER381
C	GLU382
C	ILE385
C	HOH609
D	ASN43
D	ILE44
D	ASP45
D	HOH272

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE THR D 201

Chain	Residue
C	ASN374
C	ILE375
D	ASP25
D	LYS26
D	PRO27
D	GLY28
D	GLU29
D	ALA30
D	GLN49
D	HOH204
D	HOH317

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE THR E 501

Chain	Residue
E	ASP274
E	LYS275
E	PRO276
E	ALA279
E	GLN298
F	ASN125
F	ILE126

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LYS E 601

Chain	Residue
E	MET354
E	HIS357
E	PRO358
E	GLY359
E	VAL360
E	THR361
E	THR380
E	SER381
E	GLU382
E	ILE385
F	ASN43
F	ILE44
F	ASP45

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE THR F 201

Chain	Residue
E	ASN374
E	ILE375
F	ILE23
F	ASP25
F	LYS26
F	PRO27
F	GLY28
F	GLU29
F	ALA30
F	GLN49
F	HOH606

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE THR G 501

Chain	Residue
G	ASP274
G	LYS275
G	PRO276
G	GLY277
G	GLU278
G	ALA279
G	GLN298
G	HOH608
G	HOH627
H	ASN125
H	ILE126

site_id	BC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LYS G 601

Chain	Residue
G	MET354
G	HIS357
G	PRO358
G	VAL360
G	THR361
G	SER381
G	GLU382
G	ARG384
G	ILE385
H	ASN43
H	ILE44
H	ASP45
H	HOH345

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE THR H 201

Chain	Residue
G	ASN374
G	ILE375
H	ASP25
H	LYS26
H	PRO27
H	GLY28
H	GLU29
H	ALA30
H	GLN49
H	THR59

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE THR I 501

Chain	Residue
I	ASP274
I	LYS275
I	GLY277
I	GLU278
I	ALA279
I	GLN298
I	THR308
J	ASN125
J	ILE126

site_id	BC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE THR J 201

Chain	Residue
I	ASN374
I	ILE375
J	ASP25
J	LYS26
J	GLY28
J	GLU29
J	ALA30
J	GLN49
J	THR59
J	HOH374
J	HOH375

site_id	BC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE THR K 501

Chain	Residue
K	ASP274
K	LYS275
K	GLY277
K	GLU278
K	ALA279
K	GLN298
K	HOH609
K	HOH617
L	ASN125
L	ILE126

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE LYS K 601

Chain	Residue
K	MET354
K	HIS357
K	GLY359
K	VAL360
K	THR361
K	SER381
K	HOH624
K	HOH627
L	ASN43
L	ILE44
L	ASP45

site_id	BC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE THR L 201

Chain	Residue
K	ASN374
K	ILE375
K	HOH641
L	ASP25
L	LYS26
L	PRO27
L	GLY28
L	GLU29
L	ALA30
L	GLN49
L	THR59
L	HOH202

site_id	BC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE THR M 501

Chain	Residue
M	ASP274
M	LYS275
M	PRO276
M	GLY277
M	GLU278
M	ALA279
M	GLN298
M	THR308
M	HOH613
N	ASN125
N	ILE126

site_id	CC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE LYS M 601

Chain	Residue
M	MET354
M	HIS357
M	PRO358
M	VAL360
M	THR361
M	SER381
M	GLU382
N	ASN43
N	ILE44
N	ASP45

site_id	CC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE THR N 201

Chain	Residue
M	ASN374
M	ILE375
N	ASP25
N	LYS26
N	GLY28
N	GLU29
N	ALA30
N	GLN49
N	THR59
N	HOH210
N	HOH215

site_id	CC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE THR O 501

Chain	Residue
O	LYS275
O	GLY277
O	GLU278
O	ALA279
O	GLN298
O	THR308
P	ASN125
P	ILE126

site_id	CC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE LYS O 601

Chain	Residue
O	MET354
O	LYS355
O	PRO358
O	GLY359
O	VAL360
O	THR361
O	THR380
O	SER381
O	GLU382
O	HOH605
P	ASN43
P	ILE44
P	ASP45

site_id	CC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE THR P 201

Chain	Residue
O	ASN374
O	ILE375
P	ASP25
P	LYS26
P	PRO27
P	GLY28
P	GLU29
P	ALA30
P	GLN49
P	THR59
P	HOH346

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL5-LEU13

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
B	ASP25
A	ASP274
C	LYS7
C	ARG25
C	SER41
C	GLU74
C	LEU125
C	ARG151
C	SER174
C	TYR180
C	LYS210
D	ASP25
C	ASP274
E	LYS7
E	ARG25
E	SER41
E	GLU74
E	LEU125
E	ARG151
E	SER174
E	TYR180
E	LYS210
F	ASP25
E	ASP274
G	LYS7
G	ARG25
G	SER41
G	GLU74
G	LEU125
G	ARG151
G	SER174
G	TYR180
G	LYS210
H	ASP25
G	ASP274
I	LYS7
I	ARG25
I	SER41
I	GLU74
I	LEU125
I	ARG151
I	SER174
I	TYR180
I	LYS210
J	ASP25
I	ASP274
K	LYS7
K	ARG25
K	SER41
K	GLU74
K	LEU125
K	ARG151
K	SER174
K	TYR180
K	LYS210
L	ASP25
K	ASP274
M	LYS7
M	ARG25
M	SER41
M	GLU74
M	LEU125
M	ARG151
M	SER174
M	TYR180
M	LYS210
N	ASP25
M	ASP274
O	LYS7
O	ARG25
O	SER41
O	GLU74
O	LEU125
O	ARG151
O	SER174
O	TYR180
O	LYS210
P	ASP25
O	ASP274
A	LYS210

site_id	SWS_FT_FI2
Number of Residues	40
Details	BINDING:

Chain	Residue	Details
B	ASN43
D	SER132
F	ASN43
F	GLN49
F	VAL111
F	ASN125
F	SER132
H	ASN43
H	GLN49
H	VAL111
H	ASN125
B	GLN49
H	SER132
J	ASN43
J	GLN49
J	VAL111
J	ASN125
J	SER132
L	ASN43
L	GLN49
L	VAL111
L	ASN125
B	VAL111
L	SER132
N	ASN43
N	GLN49
N	VAL111
N	ASN125
N	SER132
P	ASN43
P	GLN49
P	VAL111
P	ASN125
B	ASN125
P	SER132
K	ASN374
K	SER381
M	ASP45
M	SER154
M	ASN292
M	GLN298
M	VAL360
M	ASN374
M	SER381
B	SER132
O	ASP45
O	SER154
O	ASN292
O	GLN298
O	VAL360
O	ASN374
O	SER381
D	ASN43
D	GLN49
D	VAL111
D	ASN125

site_id	SWS_FT_FI3
Number of Residues	16
Details	SITE: Contribution to the catalysis => ECO:0000250

Chain	Residue	Details
A	LYS7
I	GLU74
K	LYS7
K	GLU74
M	LYS7
M	GLU74
O	LYS7
O	GLU74
A	GLU74
C	LYS7
C	GLU74
E	LYS7
E	GLU74
G	LYS7
G	GLU74
I	LYS7

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)