Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6VZ8

Arabidopsis thaliana acetohydroxyacid synthase complex with valine bound

Functional Information from GO Data

Chain	GOid	namespace	contents
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0003984	molecular_function	acetolactate synthase activity
D	0009082	biological_process	branched-chain amino acid biosynthetic process
D	0030976	molecular_function	thiamine pyrophosphate binding
D	0050660	molecular_function	flavin adenine dinucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0003984	molecular_function	acetolactate synthase activity
E	0009082	biological_process	branched-chain amino acid biosynthetic process
E	0030976	molecular_function	thiamine pyrophosphate binding
E	0050660	molecular_function	flavin adenine dinucleotide binding
F	0001666	biological_process	response to hypoxia
F	0003984	molecular_function	acetolactate synthase activity
F	0005515	molecular_function	protein binding
F	0005777	cellular_component	peroxisome
F	0005829	cellular_component	cytosol
F	0008652	biological_process	amino acid biosynthetic process
F	0009082	biological_process	branched-chain amino acid biosynthetic process
F	0009097	biological_process	isoleucine biosynthetic process
F	0009099	biological_process	L-valine biosynthetic process
F	0009507	cellular_component	chloroplast
F	1990610	molecular_function	acetolactate synthase regulator activity
G	0001666	biological_process	response to hypoxia
G	0003984	molecular_function	acetolactate synthase activity
G	0005515	molecular_function	protein binding
G	0005777	cellular_component	peroxisome
G	0005829	cellular_component	cytosol
G	0008652	biological_process	amino acid biosynthetic process
G	0009082	biological_process	branched-chain amino acid biosynthetic process
G	0009097	biological_process	isoleucine biosynthetic process
G	0009099	biological_process	L-valine biosynthetic process
G	0009507	cellular_component	chloroplast
G	1990610	molecular_function	acetolactate synthase regulator activity
H	0000287	molecular_function	magnesium ion binding
H	0003824	molecular_function	catalytic activity
H	0003984	molecular_function	acetolactate synthase activity
H	0009082	biological_process	branched-chain amino acid biosynthetic process
H	0030976	molecular_function	thiamine pyrophosphate binding
H	0050660	molecular_function	flavin adenine dinucleotide binding
I	0000287	molecular_function	magnesium ion binding
I	0003824	molecular_function	catalytic activity
I	0003984	molecular_function	acetolactate synthase activity
I	0009082	biological_process	branched-chain amino acid biosynthetic process
I	0030976	molecular_function	thiamine pyrophosphate binding
I	0050660	molecular_function	flavin adenine dinucleotide binding
J	0001666	biological_process	response to hypoxia
J	0003984	molecular_function	acetolactate synthase activity
J	0005515	molecular_function	protein binding
J	0005777	cellular_component	peroxisome
J	0005829	cellular_component	cytosol
J	0008652	biological_process	amino acid biosynthetic process
J	0009082	biological_process	branched-chain amino acid biosynthetic process
J	0009097	biological_process	isoleucine biosynthetic process
J	0009099	biological_process	L-valine biosynthetic process
J	0009507	cellular_component	chloroplast
J	1990610	molecular_function	acetolactate synthase regulator activity
K	0001666	biological_process	response to hypoxia
K	0003984	molecular_function	acetolactate synthase activity
K	0005515	molecular_function	protein binding
K	0005777	cellular_component	peroxisome
K	0005829	cellular_component	cytosol
K	0008652	biological_process	amino acid biosynthetic process
K	0009082	biological_process	branched-chain amino acid biosynthetic process
K	0009097	biological_process	isoleucine biosynthetic process
K	0009099	biological_process	L-valine biosynthetic process
K	0009507	cellular_component	chloroplast
K	1990610	molecular_function	acetolactate synthase regulator activity
L	0000287	molecular_function	magnesium ion binding
L	0003824	molecular_function	catalytic activity
L	0003984	molecular_function	acetolactate synthase activity
L	0009082	biological_process	branched-chain amino acid biosynthetic process
L	0030976	molecular_function	thiamine pyrophosphate binding
L	0050660	molecular_function	flavin adenine dinucleotide binding
M	0000287	molecular_function	magnesium ion binding
M	0003824	molecular_function	catalytic activity
M	0003984	molecular_function	acetolactate synthase activity
M	0009082	biological_process	branched-chain amino acid biosynthetic process
M	0030976	molecular_function	thiamine pyrophosphate binding
M	0050660	molecular_function	flavin adenine dinucleotide binding
N	0001666	biological_process	response to hypoxia
N	0003984	molecular_function	acetolactate synthase activity
N	0005515	molecular_function	protein binding
N	0005777	cellular_component	peroxisome
N	0005829	cellular_component	cytosol
N	0008652	biological_process	amino acid biosynthetic process
N	0009082	biological_process	branched-chain amino acid biosynthetic process
N	0009097	biological_process	isoleucine biosynthetic process
N	0009099	biological_process	L-valine biosynthetic process
N	0009507	cellular_component	chloroplast
N	1990610	molecular_function	acetolactate synthase regulator activity
O	0001666	biological_process	response to hypoxia
O	0003984	molecular_function	acetolactate synthase activity
O	0005515	molecular_function	protein binding
O	0005777	cellular_component	peroxisome
O	0005829	cellular_component	cytosol
O	0008652	biological_process	amino acid biosynthetic process
O	0009082	biological_process	branched-chain amino acid biosynthetic process
O	0009097	biological_process	isoleucine biosynthetic process
O	0009099	biological_process	L-valine biosynthetic process
O	0009507	cellular_component	chloroplast
O	1990610	molecular_function	acetolactate synthase regulator activity
P	0000287	molecular_function	magnesium ion binding
P	0003824	molecular_function	catalytic activity
P	0003984	molecular_function	acetolactate synthase activity
P	0009082	biological_process	branched-chain amino acid biosynthetic process
P	0030976	molecular_function	thiamine pyrophosphate binding
P	0050660	molecular_function	flavin adenine dinucleotide binding
Q	0000287	molecular_function	magnesium ion binding
Q	0003824	molecular_function	catalytic activity
Q	0003984	molecular_function	acetolactate synthase activity
Q	0009082	biological_process	branched-chain amino acid biosynthetic process
Q	0030976	molecular_function	thiamine pyrophosphate binding
Q	0050660	molecular_function	flavin adenine dinucleotide binding
R	0001666	biological_process	response to hypoxia
R	0003984	molecular_function	acetolactate synthase activity
R	0005515	molecular_function	protein binding
R	0005777	cellular_component	peroxisome
R	0005829	cellular_component	cytosol
R	0008652	biological_process	amino acid biosynthetic process
R	0009082	biological_process	branched-chain amino acid biosynthetic process
R	0009097	biological_process	isoleucine biosynthetic process
R	0009099	biological_process	L-valine biosynthetic process
R	0009507	cellular_component	chloroplast
R	1990610	molecular_function	acetolactate synthase regulator activity
S	0001666	biological_process	response to hypoxia
S	0003984	molecular_function	acetolactate synthase activity
S	0005515	molecular_function	protein binding
S	0005777	cellular_component	peroxisome
S	0005829	cellular_component	cytosol
S	0008652	biological_process	amino acid biosynthetic process
S	0009082	biological_process	branched-chain amino acid biosynthetic process
S	0009097	biological_process	isoleucine biosynthetic process
S	0009099	biological_process	L-valine biosynthetic process
S	0009507	cellular_component	chloroplast
S	1990610	molecular_function	acetolactate synthase regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue MG D 701

Chain	Residue
D	HIS567
D	LEU568
D	GLY569
D	TPP703

site_id	AC2
Number of Residues	19
Details	binding site for residue FAD D 702

Chain	Residue
D	LEU332
D	MET333
D	LEU349
D	GLY350
D	MET351
D	HIS352
D	ARG373
D	ASP375
D	ARG377
D	VAL378
D	ASP395
D	ILE396
D	GLN489
D	GLY508
D	ARG246
D	GLY307
D	GLY308
D	GLY309
D	THR331

site_id	AC3
Number of Residues	20
Details	binding site for residue TPP D 703

Chain	Residue
D	VAL485
D	GLY486
D	GLN487
D	HIS488
D	GLY511
D	MET513
D	GLY537
D	ASP538
D	GLY539
D	SER540
D	ASN565
D	HIS567
D	LEU568
D	GLY569
D	MET570
D	VAL571
D	MG701
E	GLU144
E	PRO170
E	GLN207

site_id	AC4
Number of Residues	4
Details	binding site for residue MG E 701

Chain	Residue
E	GLY537
E	ASP538
E	HIS567
E	TPP703

site_id	AC5
Number of Residues	21
Details	binding site for residue FAD E 702

Chain	Residue
E	LEU184
E	GLY307
E	GLY308
E	GLY309
E	THR331
E	LEU332
E	MET333
E	LEU349
E	GLY350
E	MET351
E	HIS352
E	VAL372
E	ARG373
E	ARG377
E	ASP395
E	ILE396
E	ASP397
E	ASP414
E	VAL415
E	GLY508
E	GLY509

site_id	AC6
Number of Residues	19
Details	binding site for residue TPP E 703

Chain	Residue
D	GLU144
D	PRO170
D	GLN207
E	VAL485
E	GLY486
E	GLN487
E	HIS488
E	GLY511
E	MET513
E	GLY537
E	ASP538
E	GLY539
E	SER540
E	ASN565
E	LEU568
E	GLY569
E	MET570
E	VAL571
E	MG701

site_id	AC7
Number of Residues	7
Details	binding site for residue VAL F 501

Chain	Residue
F	ASP95
F	GLU96
F	GLY98
F	MET99
F	ILE100
G	ASN346
G	ILE347

site_id	AC8
Number of Residues	8
Details	binding site for residue VAL G 501

Chain	Residue
G	VAL332
G	LEU333
G	SER361
F	ASN113
F	ILE114
G	ASP328
G	ILE329
G	GLY331

site_id	AC9
Number of Residues	4
Details	binding site for residue MG H 701

Chain	Residue
H	HIS567
H	LEU568
H	GLY569
H	TPP703

site_id	AD1
Number of Residues	19
Details	binding site for residue FAD H 702

Chain	Residue
H	ARG246
H	GLY307
H	GLY308
H	GLY309
H	THR331
H	LEU332
H	MET333
H	LEU349
H	GLY350
H	MET351
H	HIS352
H	ARG373
H	ASP375
H	ARG377
H	VAL378
H	ASP395
H	ILE396
H	GLN489
H	GLY508

site_id	AD2
Number of Residues	20
Details	binding site for residue TPP H 703

Chain	Residue
H	VAL485
H	GLY486
H	GLN487
H	HIS488
H	GLY511
H	MET513
H	GLY537
H	ASP538
H	GLY539
H	SER540
H	ASN565
H	HIS567
H	LEU568
H	GLY569
H	MET570
H	VAL571
H	MG701
I	GLU144
I	PRO170
I	GLN207

site_id	AD3
Number of Residues	4
Details	binding site for residue MG I 701

Chain	Residue
I	GLY537
I	ASP538
I	HIS567
I	TPP703

site_id	AD4
Number of Residues	21
Details	binding site for residue FAD I 702

Chain	Residue
I	LEU184
I	GLY307
I	GLY308
I	GLY309
I	THR331
I	LEU332
I	MET333
I	LEU349
I	GLY350
I	MET351
I	HIS352
I	VAL372
I	ARG373
I	ARG377
I	ASP395
I	ILE396
I	ASP397
I	ASP414
I	VAL415
I	GLY508
I	GLY509

site_id	AD5
Number of Residues	19
Details	binding site for residue TPP I 703

Chain	Residue
H	GLU144
H	PRO170
H	GLN207
I	VAL485
I	GLY486
I	GLN487
I	HIS488
I	GLY511
I	MET513
I	GLY537
I	ASP538
I	GLY539
I	SER540
I	ASN565
I	LEU568
I	GLY569
I	MET570
I	VAL571
I	MG701

site_id	AD6
Number of Residues	6
Details	binding site for residue VAL J 501

Chain	Residue
J	ASP95
J	GLU96
J	MET99
J	ILE100
K	ASN346
K	ILE347

site_id	AD7
Number of Residues	7
Details	binding site for residue VAL K 501

Chain	Residue
J	ASN113
J	ILE114
K	ASP328
K	GLY331
K	VAL332
K	LEU333
K	SER361

site_id	AD8
Number of Residues	4
Details	binding site for residue MG L 701

Chain	Residue
L	HIS567
L	LEU568
L	GLY569
L	TPP703

site_id	AD9
Number of Residues	19
Details	binding site for residue FAD L 702

Chain	Residue
L	ARG246
L	GLY307
L	GLY308
L	GLY309
L	THR331
L	LEU332
L	MET333
L	LEU349
L	GLY350
L	MET351
L	HIS352
L	ARG373
L	ASP375
L	ARG377
L	VAL378
L	ASP395
L	ILE396
L	GLN489
L	GLY508

site_id	AE1
Number of Residues	20
Details	binding site for residue TPP L 703

Chain	Residue
L	VAL485
L	GLY486
L	GLN487
L	HIS488
L	GLY511
L	MET513
L	GLY537
L	ASP538
L	GLY539
L	SER540
L	ASN565
L	HIS567
L	LEU568
L	GLY569
L	MET570
L	VAL571
L	MG701
M	GLU144
M	PRO170
M	GLN207

site_id	AE2
Number of Residues	4
Details	binding site for residue MG M 701

Chain	Residue
M	GLY537
M	ASP538
M	HIS567
M	TPP703

site_id	AE3
Number of Residues	21
Details	binding site for residue FAD M 702

Chain	Residue
M	LEU184
M	GLY307
M	GLY308
M	GLY309
M	THR331
M	LEU332
M	MET333
M	LEU349
M	GLY350
M	MET351
M	HIS352
M	VAL372
M	ARG373
M	ARG377
M	ASP395
M	ILE396
M	ASP397
M	ASP414
M	VAL415
M	GLY508
M	GLY509

site_id	AE4
Number of Residues	19
Details	binding site for residue TPP M 703

Chain	Residue
L	GLU144
L	PRO170
L	GLN207
M	VAL485
M	GLY486
M	GLN487
M	HIS488
M	GLY511
M	MET513
M	GLY537
M	ASP538
M	GLY539
M	SER540
M	ASN565
M	LEU568
M	GLY569
M	MET570
M	VAL571
M	MG701

site_id	AE5
Number of Residues	7
Details	binding site for residue VAL N 501

Chain	Residue
N	ASP95
N	GLU96
N	GLY98
N	MET99
N	ILE100
O	ASN346
O	ILE347

site_id	AE6
Number of Residues	8
Details	binding site for residue VAL O 501

Chain	Residue
N	ASN113
N	ILE114
O	ASP328
O	ILE329
O	GLY331
O	VAL332
O	LEU333
O	SER361

site_id	AE7
Number of Residues	4
Details	binding site for residue MG P 701

Chain	Residue
P	HIS567
P	LEU568
P	GLY569
P	TPP703

site_id	AE8
Number of Residues	19
Details	binding site for residue FAD P 702

Chain	Residue
P	ARG246
P	GLY307
P	GLY308
P	GLY309
P	THR331
P	LEU332
P	MET333
P	LEU349
P	GLY350
P	MET351
P	HIS352
P	ARG373
P	ASP375
P	ARG377
P	VAL378
P	ASP395
P	ILE396
P	GLN489
P	GLY508

site_id	AE9
Number of Residues	20
Details	binding site for residue TPP P 703

Chain	Residue
P	VAL485
P	GLY486
P	GLN487
P	HIS488
P	GLY511
P	MET513
P	GLY537
P	ASP538
P	GLY539
P	SER540
P	ASN565
P	HIS567
P	LEU568
P	GLY569
P	MET570
P	VAL571
P	MG701
Q	GLU144
Q	PRO170
Q	GLN207

site_id	AF1
Number of Residues	4
Details	binding site for residue MG Q 701

Chain	Residue
Q	GLY537
Q	ASP538
Q	HIS567
Q	TPP703

site_id	AF2
Number of Residues	21
Details	binding site for residue FAD Q 702

Chain	Residue
Q	LEU184
Q	GLY307
Q	GLY308
Q	GLY309
Q	THR331
Q	LEU332
Q	MET333
Q	LEU349
Q	GLY350
Q	MET351
Q	HIS352
Q	VAL372
Q	ARG373
Q	ARG377
Q	ASP395
Q	ILE396
Q	ASP397
Q	ASP414
Q	VAL415
Q	GLY508
Q	GLY509

site_id	AF3
Number of Residues	19
Details	binding site for residue TPP Q 703

Chain	Residue
P	GLU144
P	PRO170
P	GLN207
Q	VAL485
Q	GLY486
Q	GLN487
Q	HIS488
Q	GLY511
Q	MET513
Q	GLY537
Q	ASP538
Q	GLY539
Q	SER540
Q	ASN565
Q	LEU568
Q	GLY569
Q	MET570
Q	VAL571
Q	MG701

site_id	AF4
Number of Residues	7
Details	binding site for residue VAL R 501

Chain	Residue
R	ASP95
R	GLU96
R	GLY98
R	MET99
R	ILE100
S	ASN346
S	ILE347

site_id	AF5
Number of Residues	8
Details	binding site for residue VAL S 501

Chain	Residue
R	ASN113
R	ILE114
S	ASP328
S	ILE329
S	GLY331
S	VAL332
S	LEU333
S	SER361

Functional Information from PROSITE/UniProt

site_id	PS00187
Number of Residues	20
Details	TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGasvanPdaivVdIdGDGS

Chain	Residue	Details
D	ILE521-SER540

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16407096","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32640464","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6U9H","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16407096","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Z8N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16407096","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YBH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	88
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16407096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32640464","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6U9H","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32640464","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VZ8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16407096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19187232","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32640464","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6U9H","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16407096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19187232","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16407096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19187232","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32640464","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6VZ8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Modified residue: {"description":"Cysteine sulfinic acid (-SO2H)","evidences":[{"source":"PubMed","id":"16407096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19187232","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	128
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	288
Details	Domain: {"description":"ACT 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01007","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	296
Details	Domain: {"description":"ACT 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01007","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)