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1T9B

Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0003984molecular_functionacetolactate synthase activity
A0005739cellular_componentmitochondrion
A0005948cellular_componentacetolactate synthase complex
A0008652biological_processamino acid biosynthetic process
A0009082biological_processbranched-chain amino acid biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0009099biological_processvaline biosynthetic process
A0016740molecular_functiontransferase activity
A0030976molecular_functionthiamine pyrophosphate binding
A0046872molecular_functionmetal ion binding
A0050660molecular_functionflavin adenine dinucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0003984molecular_functionacetolactate synthase activity
B0005739cellular_componentmitochondrion
B0005948cellular_componentacetolactate synthase complex
B0008652biological_processamino acid biosynthetic process
B0009082biological_processbranched-chain amino acid biosynthetic process
B0009097biological_processisoleucine biosynthetic process
B0009099biological_processvaline biosynthetic process
B0016740molecular_functiontransferase activity
B0030976molecular_functionthiamine pyrophosphate binding
B0046872molecular_functionmetal ion binding
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 696
ChainResidue
BGLN343
BASP350
BGLN506
BTRP508
BHOH4232
BHOH5202

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 699
ChainResidue
BP25698
BHOH4246
BASP550
BASN577
BGLU579

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 1696
ChainResidue
AGLN343
AASP350
AGLN506
ATRP508
AHOH4034
AHOH4492

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1699
ChainResidue
AASP550
AASN577
AGLU579
AP221702
AHOH4051

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1CS A 695
ChainResidue
AASP379
AARG380
AMET582
ATRP586
AFAD701
AHOH4808
AHOH5138
BGLY116
BVAL191
BALA200
BPHE201

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE P25 B 698
ChainResidue
ANSP704
BVAL497
BGLY498
BGLN499
BHIS500
BMET525
BGLY549
BASP550
BALA551
BSER552
BASN577
BGLU579
BGLN580
BGLY581
BMET582
BMG699
BHOH4246

site_idAC7
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD A 701
ChainResidue
AASP180
AARG241
AGLY307
AALA308
AGLY309
AASN312
ATHR334
ALEU335
ALEU352
AMET354
AHIS355
AGLY374
AALA375
AARG376
AASP378
AARG380
AVAL381
AGLU407
AVAL408
ASER409
AASN412
AGLY425
AASP426
AALA427
AGLN501
AMET502
ASER519
AGLY520
AGLY521
A1CS695
AHOH4014
AHOH4015
AHOH4031
AHOH4144
AHOH4325
AHOH4534
BPHE201

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NSP A 704
ChainResidue
AGLU139
APRO165
AASN169
AGLN202
BGLY523
BMET525
BMET555
BVAL583
BP25698
BHOH4820

site_idAC9
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 1CS B 1695
ChainResidue
APRO192
AALA200
APHE201
ALYS251
AHOH4076
BMET354
BASP379
BARG380
BMET582
BTRP586
BFAD1701
BHOH4593
BHOH4816
AGLY116
AVAL191

site_idBC1
Number of Residues40
DetailsBINDING SITE FOR RESIDUE FAD B 1701
ChainResidue
APHE201
BASP180
BARG241
BGLY307
BALA308
BGLY309
BASN312
BTHR334
BLEU335
BGLN336
BMET351
BLEU352
BGLY353
BMET354
BHIS355
BGLY374
BALA375
BARG376
BASP378
BARG380
BVAL381
BPHE406
BGLU407
BVAL408
BASN412
BGLY425
BASP426
BALA427
BGLN501
BMET502
BSER519
BGLY520
BGLY521
B1CS1695
BHOH4204
BHOH4212
BHOH4229
BHOH4259
BHOH4539
BHOH5172

site_idBC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE P22 A 1702
ChainResidue
AVAL497
AGLY498
AGLN499
AHIS500
AGLY549
AASP550
AALA551
ASER552
AASN577
AGLU579
AGLN580
AGLY581
AMET582
AMG1699
AYF31705
AHOH4051

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE YF3 A 1705
ChainResidue
AGLY523
AMET525
AMET555
AGLN580
AVAL583
AP221702
BTYR113
BPRO114
BGLU139
BPRO165
BASN169
BGLN202

Functional Information from PROSITE/UniProt
site_idPS00187
Number of Residues20
DetailsTPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGaqvakPeslvIdIdGDAS
ChainResidueDetails
AILE533-SER552

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLU139
AASP550
AASN577
AGLU579
BGLU139
BASP550
BASN577
BGLU579

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12496246
ChainResidueDetails
AARG241
AHIS355
AGLU407
BARG241
BHIS355
BGLU407

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
AVAL651

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BVAL651

site_idMCSA1
Number of Residues5
DetailsM-CSA 289
ChainResidueDetails
AGLU139hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
APHE201single electron acceptor, single electron donor, single electron relay
AGLN202electrostatic stabiliser, hydrogen bond donor
ALYS251steric locator
AMET582polar interaction, steric role

site_idMCSA2
Number of Residues5
DetailsM-CSA 289
ChainResidueDetails
BGLU139hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BPHE201single electron acceptor, single electron donor, single electron relay
BGLN202electrostatic stabiliser, hydrogen bond donor
BLYS251steric locator
BMET582polar interaction, steric role

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PDB entries from 2024-07-10

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