Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1T9D

Crystal Structure Of Yeast Acetohydroxyacid Synthase In Complex With A Sulfonylurea Herbicide, Metsulfuron methyl

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0003984	molecular_function	acetolactate synthase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005948	cellular_component	acetolactate synthase complex
A	0008652	biological_process	amino acid biosynthetic process
A	0009082	biological_process	branched-chain amino acid biosynthetic process
A	0009097	biological_process	isoleucine biosynthetic process
A	0009099	biological_process	L-valine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0003984	molecular_function	acetolactate synthase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005948	cellular_component	acetolactate synthase complex
B	0008652	biological_process	amino acid biosynthetic process
B	0009082	biological_process	branched-chain amino acid biosynthetic process
B	0009097	biological_process	isoleucine biosynthetic process
B	0009099	biological_process	L-valine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0030976	molecular_function	thiamine pyrophosphate binding
B	0046872	molecular_function	metal ion binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0003984	molecular_function	acetolactate synthase activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005948	cellular_component	acetolactate synthase complex
C	0008652	biological_process	amino acid biosynthetic process
C	0009082	biological_process	branched-chain amino acid biosynthetic process
C	0009097	biological_process	isoleucine biosynthetic process
C	0009099	biological_process	L-valine biosynthetic process
C	0016740	molecular_function	transferase activity
C	0030976	molecular_function	thiamine pyrophosphate binding
C	0046872	molecular_function	metal ion binding
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0003984	molecular_function	acetolactate synthase activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005948	cellular_component	acetolactate synthase complex
D	0008652	biological_process	amino acid biosynthetic process
D	0009082	biological_process	branched-chain amino acid biosynthetic process
D	0009097	biological_process	isoleucine biosynthetic process
D	0009099	biological_process	L-valine biosynthetic process
D	0016740	molecular_function	transferase activity
D	0030976	molecular_function	thiamine pyrophosphate binding
D	0046872	molecular_function	metal ion binding
D	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 696

Chain	Residue
B	GLN343
B	ASP350
B	GLN506
B	TRP508
B	HOH4274
B	HOH5858

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 699

Chain	Residue
B	P25698
B	HOH4287
B	ASP550
B	ASN577
B	GLU579

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 1696

Chain	Residue
A	GLN343
A	ASP350
A	GLN506
A	TRP508
A	HOH4043
A	HOH5543

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1699

Chain	Residue
A	ASP550
A	ASN577
A	GLU579
A	P251698
A	HOH4061

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K D 2696

Chain	Residue
D	GLN343
D	ASP350
D	GLN506
D	TRP508
D	HOH4801
D	HOH5353

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 2699

Chain	Residue
D	ASP550
D	ASN577
D	GLU579
D	P222702
D	HOH4819

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K C 3696

Chain	Residue
C	GLN343
C	ASP350
C	GLN506
C	TRP508
C	HOH5037

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 3699

Chain	Residue
C	ASP550
C	ASN577
C	GLU579
C	P223702
C	HOH5774

site_id	AC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 1MM A 695

Chain	Residue
A	MET354
A	ASP379
A	ARG380
A	MET582
A	TRP586
A	FAD701
A	HOH4173
B	GLY116
B	ALA117
B	VAL191
B	PRO192
B	PHE201
B	GLN202
B	LYS251
B	HOH4143

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE P25 B 698

Chain	Residue
B	VAL497
B	GLY498
B	GLN499
B	HIS500
B	GLY549
B	ASP550
B	ALA551
B	SER552
B	ASN577
B	GLU579
B	GLN580
B	GLY581
B	MET582
B	MG699
B	HOH4287

site_id	BC2
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD A 701

Chain	Residue
A	VAL497
A	GLN501
A	MET502
A	GLY520
A	GLY521
A	1MM695
A	HOH4015
A	HOH4016
A	HOH4037
A	HOH4160
A	HOH5915
A	HOH6042
B	PHE201
A	ASP180
A	ARG241
A	GLY307
A	ALA308
A	GLY309
A	ASN312
A	THR334
A	LEU335
A	GLN336
A	LEU352
A	GLY353
A	MET354
A	HIS355
A	GLY374
A	ALA375
A	ARG376
A	ASP378
A	ARG380
A	VAL381
A	PHE406
A	GLU407
A	VAL408
A	ASN412
A	GLY425
A	ASP426
A	ALA427

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PYD A 703

Chain	Residue
A	GLY115
A	GLU139
A	PRO165
A	ASN169
A	GLN202
B	GLY523
B	MET525
B	MET555
B	GLN580

site_id	BC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 1MM B 1695

Chain	Residue
A	GLY116
A	ALA117
A	VAL191
A	PRO192
A	ALA200
A	PHE201
A	GLN202
A	LYS251
B	ASP379
B	ARG380
B	MET582
B	VAL583
B	TRP586
B	FAD1701
B	HOH5600

site_id	BC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE P25 A 1698

Chain	Residue
A	VAL497
A	GLY498
A	GLN499
A	HIS500
A	MET525
A	GLY549
A	ASP550
A	ALA551
A	SER552
A	ASN577
A	GLU579
A	GLN580
A	GLY581
A	MET582
A	MG1699
A	HOH4061

site_id	BC6
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD B 1701

Chain	Residue
A	PHE201
B	ASP180
B	ARG241
B	GLY307
B	ALA308
B	GLY309
B	ASN312
B	THR334
B	LEU335
B	GLN336
B	LEU352
B	MET354
B	HIS355
B	GLY374
B	ALA375
B	ARG376
B	ASP378
B	ARG380
B	VAL381
B	PHE406
B	GLU407
B	VAL408
B	ASN412
B	GLY425
B	ASP426
B	ALA427
B	GLN501
B	MET502
B	SER519
B	GLY520
B	GLY521
B	MET582
B	1MM1695
B	HOH4248
B	HOH4270
B	HOH4302
B	HOH4615
B	HOH5940
B	HOH5956

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PYD B 1703

Chain	Residue
A	GLY523
A	MET525
A	MET555
B	PRO114
B	GLY115
B	GLU139
B	PRO165
B	ASN169
B	GLN202

site_id	BC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 1MM C 2695

Chain	Residue
C	GLY116
C	ALA117
C	VAL191
C	PRO192
C	PHE201
C	LYS251
C	HOH4890
C	HOH4944
C	HOH5740
D	MET354
D	ASP379
D	ARG380
D	TRP586
D	FAD3701

site_id	BC9
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD C 2701

Chain	Residue
C	ARG241
C	GLY307
C	ALA308
C	GLY309
C	ASN312
C	THR334
C	LEU335
C	LEU352
C	GLY353
C	MET354
C	HIS355
C	GLY374
C	ALA375
C	ARG376
C	ASP378
C	ARG380
C	VAL381
C	PHE406
C	GLU407
C	VAL408
C	ASN412
C	GLY425
C	ASP426
C	ALA427
C	GLN501
C	MET502
C	SER519
C	GLY520
C	GLY521
C	1MM3695
C	HOH5008
C	HOH5017
C	HOH5034
C	HOH5067
C	HOH5764
C	HOH6001
D	PHE201

site_id	CC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE P22 D 2702

Chain	Residue
D	VAL497
D	GLY498
D	GLN499
D	HIS500
D	MET525
D	GLY549
D	ASP550
D	ALA551
D	SER552
D	ASN577
D	GLU579
D	GLN580
D	GLY581
D	MET582
D	MG2699
D	HOH4819

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PYD C 2703

Chain	Residue
C	PRO114
C	GLY115
C	GLU139
C	PRO165
C	ASN169
C	GLN202
D	GLY523
D	MET525

site_id	CC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 1MM C 3695

Chain	Residue
C	MET354
C	ASP379
C	ARG380
C	MET582
C	VAL583
C	TRP586
C	FAD2701
C	HOH4789
C	HOH5408
D	GLY116
D	ALA117
D	VAL191
D	PRO192
D	PHE201
D	GLN202
D	LYS251

site_id	CC4
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD D 3701

Chain	Residue
C	PHE201
C	1MM2695
D	ASP180
D	ARG241
D	GLY307
D	ALA308
D	GLY309
D	ASN312
D	THR334
D	LEU335
D	GLN336
D	LEU352
D	GLY353
D	MET354
D	HIS355
D	GLY374
D	ALA375
D	ARG376
D	ASP378
D	ARG380
D	VAL381
D	PHE406
D	GLU407
D	VAL408
D	ASN412
D	GLY425
D	ASP426
D	ALA427
D	GLN501
D	MET502
D	SER519
D	GLY520
D	GLY521
D	HOH4774
D	HOH4775
D	HOH4795
D	HOH4873
D	HOH4926
D	HOH5146

site_id	CC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE P22 C 3702

Chain	Residue
C	VAL497
C	GLY498
C	GLN499
C	HIS500
C	MET525
C	GLY549
C	ASP550
C	ALA551
C	SER552
C	ASN577
C	GLU579
C	GLN580
C	GLY581
C	MET582
C	MG3699
C	HOH5774

site_id	CC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PYD D 3703

Chain	Residue
C	VAL497
C	GLY523
C	MET525
D	PRO114
D	GLY115
D	GLU139
D	PRO165
D	ASN169
D	GLN202

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE533-SER552

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	320
Details	Region: {"description":"Thiamine pyrophosphate binding"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	164
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12496246","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	VAL651

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

Chain	Residue	Details
B	VAL651

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

Chain	Residue	Details
C	VAL651

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

Chain	Residue	Details
D	VAL651

site_id	MCSA1
Number of Residues	5
Details	M-CSA 289

Chain	Residue	Details
A	GLU139	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	PHE201	single electron acceptor, single electron donor, single electron relay
A	GLN202	electrostatic stabiliser, hydrogen bond donor
A	LYS251	steric locator
A	MET582	polar interaction, steric role

site_id	MCSA2
Number of Residues	5
Details	M-CSA 289

Chain	Residue	Details
B	GLU139	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	PHE201	single electron acceptor, single electron donor, single electron relay
B	GLN202	electrostatic stabiliser, hydrogen bond donor
B	LYS251	steric locator
B	MET582	polar interaction, steric role

site_id	MCSA3
Number of Residues	5
Details	M-CSA 289

Chain	Residue	Details
C	GLU139	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	PHE201	single electron acceptor, single electron donor, single electron relay
C	GLN202	electrostatic stabiliser, hydrogen bond donor
C	LYS251	steric locator
C	MET582	polar interaction, steric role

site_id	MCSA4
Number of Residues	5
Details	M-CSA 289

Chain	Residue	Details
D	GLU139	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	PHE201	single electron acceptor, single electron donor, single electron relay
D	GLN202	electrostatic stabiliser, hydrogen bond donor
D	LYS251	steric locator
D	MET582	polar interaction, steric role

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