Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5WKC

Saccharomyces cerevisiae acetohydroxyacid synthase in complex with the herbicide penoxsulam

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	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	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	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	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
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0003984	molecular_function	acetolactate synthase activity
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	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
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0003984	molecular_function	acetolactate synthase activity
E	0005739	cellular_component	mitochondrion
E	0005948	cellular_component	acetolactate synthase complex
E	0008652	biological_process	amino acid biosynthetic process
E	0009082	biological_process	branched-chain amino acid biosynthetic process
E	0009097	biological_process	isoleucine biosynthetic process
E	0009099	biological_process	valine biosynthetic process
E	0016740	molecular_function	transferase activity
E	0030976	molecular_function	thiamine pyrophosphate binding
E	0046872	molecular_function	metal ion binding
E	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 701

Chain	Residue
A	ASP550
A	ASN577
A	GLU579
A	AUJ705
A	HOH845

site_id	AC2
Number of Residues	15
Details	binding site for residue PXD A 702

Chain	Residue
A	VAL583
A	TRP586
A	FAD703
A	AUJ705
D	GLY116
D	ALA117
D	SER163
D	VAL191
D	PHE201
D	LYS251
D	HOH947
A	MET354
A	ASP379
A	ARG380
A	MET582

site_id	AC3
Number of Residues	36
Details	binding site for residue FAD A 703

Chain	Residue
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	ARG380
A	VAL381
A	GLU407
A	VAL408
A	ASN412
A	GLY425
A	ASP426
A	ALA427
A	GLN501
A	MET502
A	GLY520
A	GLY521
A	PXD702
A	HOH828
A	HOH831
A	HOH856
A	HOH863
A	HOH923
A	HOH937
D	PHE201

site_id	AC4
Number of Residues	6
Details	binding site for residue F50 A 704

Chain	Residue
A	GLY115
A	GLY116
A	GLN202
D	MET582
D	PXD702
D	TP9704

site_id	AC5
Number of Residues	26
Details	binding site for residue AUJ A 705

Chain	Residue
A	VAL497
A	GLY498
A	GLN499
A	HIS500
A	GLY523
A	MET525
A	GLY549
A	ASP550
A	ALA551
A	SER552
A	ASN577
A	GLU579
A	GLN580
A	GLY581
A	MET582
A	VAL583
A	MG701
A	PXD702
A	HOH845
D	TYR113
D	PRO114
D	GLY116
D	GLU139
D	PRO165
D	ASN169
D	GLN202

site_id	AC6
Number of Residues	5
Details	binding site for residue MG B 701

Chain	Residue
B	ASP550
B	ASN577
B	GLU579
B	TP9704
B	HOH897

site_id	AC7
Number of Residues	16
Details	binding site for residue PXD B 702

Chain	Residue
B	FAD703
B	HOH1001
B	HOH1060
E	GLY116
E	ALA117
E	VAL191
E	PHE201
E	LYS251
E	F50705
E	HOH804
B	MET354
B	ASP379
B	ARG380
B	MET582
B	VAL583
B	TRP586

site_id	AC8
Number of Residues	34
Details	binding site for residue FAD B 703

Chain	Residue
B	ARG241
B	GLY307
B	ALA308
B	GLY309
B	ASN312
B	THR334
B	LEU335
B	GLN336
B	LEU352
B	GLY353
B	MET354
B	HIS355
B	GLY374
B	ALA375
B	ARG376
B	ARG380
B	VAL381
B	GLU407
B	VAL408
B	ASN412
B	GLY425
B	ASP426
B	ALA427
B	GLN501
B	MET502
B	GLY520
B	GLY521
B	PXD702
B	HOH852
B	HOH889
B	HOH946
B	HOH989
B	HOH1050
E	PHE201

site_id	AC9
Number of Residues	24
Details	binding site for residue TP9 B 704

Chain	Residue
B	VAL497
B	GLY498
B	GLN499
B	HIS500
B	GLY523
B	MET525
B	GLY549
B	ASP550
B	ALA551
B	SER552
B	ASN577
B	GLU579
B	GLN580
B	GLY581
B	MET582
B	VAL583
B	MG701
B	HOH897
E	TYR113
E	PRO114
E	GLU139
E	ASN169
E	GLN202
E	F50705

site_id	AD1
Number of Residues	6
Details	binding site for residue F50 B 705

Chain	Residue
B	GLY115
B	GLY116
B	GLN202
E	MET582
E	PXD702
E	TP9704

site_id	AD2
Number of Residues	5
Details	binding site for residue MG E 701

Chain	Residue
E	ASP550
E	ASN577
E	GLU579
E	TP9704
E	HOH831

site_id	AD3
Number of Residues	13
Details	binding site for residue PXD E 702

Chain	Residue
B	GLY116
B	ALA117
B	VAL191
B	PHE201
B	LYS251
B	F50705
E	MET354
E	ASP379
E	ARG380
E	MET582
E	VAL583
E	TRP586
E	FAD703

site_id	AD4
Number of Residues	35
Details	binding site for residue FAD E 703

Chain	Residue
B	PHE201
E	ASP180
E	ARG241
E	GLY307
E	ALA308
E	GLY309
E	ASN312
E	THR334
E	LEU335
E	GLN336
E	LEU352
E	GLY353
E	MET354
E	HIS355
E	GLY374
E	ALA375
E	ARG376
E	ARG380
E	VAL381
E	GLU407
E	VAL408
E	ASN412
E	GLY425
E	ASP426
E	ALA427
E	GLN501
E	MET502
E	GLY520
E	GLY521
E	PXD702
E	HOH809
E	HOH821
E	HOH835
E	HOH895
E	HOH918

site_id	AD5
Number of Residues	24
Details	binding site for residue TP9 E 704

Chain	Residue
B	PRO114
B	GLU139
B	PRO165
B	ASN169
B	GLN202
B	F50705
E	VAL497
E	GLY498
E	GLN499
E	HIS500
E	GLY523
E	MET525
E	GLY549
E	ASP550
E	ALA551
E	SER552
E	ASN577
E	GLU579
E	GLN580
E	GLY581
E	MET582
E	VAL583
E	MG701
E	HOH831

site_id	AD6
Number of Residues	5
Details	binding site for residue F50 E 705

Chain	Residue
B	MET582
B	PXD702
B	TP9704
E	GLY116
E	GLN202

site_id	AD7
Number of Residues	5
Details	binding site for residue MG D 701

Chain	Residue
D	ASP550
D	ASN577
D	GLU579
D	TP9704
D	HOH922

site_id	AD8
Number of Residues	15
Details	binding site for residue PXD D 702

Chain	Residue
A	GLY116
A	ALA117
A	VAL191
A	PHE201
A	LYS251
A	F50704
A	HOH822
D	MET354
D	ASP379
D	ARG380
D	MET582
D	VAL583
D	TRP586
D	FAD703
D	HOH1066

site_id	AD9
Number of Residues	36
Details	binding site for residue FAD D 703

Chain	Residue
A	PHE201
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	ARG380
D	VAL381
D	GLU407
D	VAL408
D	ASN412
D	GLY425
D	ASP426
D	ALA427
D	GLN501
D	SME502
D	GLY520
D	GLY521
D	MET582
D	PXD702
D	HOH815
D	HOH877
D	HOH890
D	HOH944
D	HOH1005

site_id	AE1
Number of Residues	25
Details	binding site for residue TP9 D 704

Chain	Residue
A	TYR113
A	PRO114
A	GLU139
A	PRO165
A	ASN169
A	GLN202
A	F50704
D	VAL497
D	GLY498
D	GLN499
D	HIS500
D	GLY523
D	MET525
D	GLY549
D	ASP550
D	ALA551
D	SER552
D	ASN577
D	GLU579
D	GLN580
D	GLY581
D	MET582
D	VAL583
D	MG701
D	HOH922

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
D	ILE533-SER552
A	ILE533-SER552

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
D	GLU139
E	ASP550
E	ASN577
E	GLU579
D	ASP550
D	ASN577
D	GLU579
B	GLU139
B	ASP550
B	ASN577
B	GLU579
E	GLU139

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:12496246

Chain	Residue	Details
D	ARG241
D	HIS355
D	GLU407
B	ARG241
B	HIS355
B	GLU407
E	ARG241
E	HIS355
E	GLU407

Catalytic Information from CSA

site_id	MCSA1
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

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

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