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6BD3

Saccharomyces cerevisiae acetohydroxyacid synthase

Replaces:  5INV
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 A 701
ChainResidue
AGLN343
AASP350
AGLN506
ATRP508
AHOH809
AHOH893

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 702
ChainResidue
AHOH834
AHOH891
AASP550
AASN577
ATPP703

site_idAC3
Number of Residues20
Detailsbinding site for residue TPP A 703
ChainResidue
AVAL497
AGLY498
AGLN499
AHIS500
AGLY523
AMET525
AASP550
AALA551
ASER552
AASN577
AMG702
AHOH834
AHOH891
AHOH948
BPRO114
BGLU139
BPRO165
BASN169
BGLN202
BACT712

site_idAC4
Number of Residues6
Detailsbinding site for residue OXY A 704
ChainResidue
AALA551
AGLN600
AHOH811
AHOH833
BTYR113
BLYS137

site_idAC5
Number of Residues8
Detailsbinding site for residue OXY A 705
ChainResidue
AGLY115
AGLY116
AALA117
ATHR162
ASER163
AGLN202
ACO2706
AHOH939

site_idAC6
Number of Residues5
Detailsbinding site for residue CO2 A 706
ChainResidue
AGLY116
AOXY705
AHOH939
BHTL703
BOXY704

site_idAC7
Number of Residues29
Detailsbinding site for residue FAD A 707
ChainResidue
AARG241
AGLY307
AALA308
AGLY309
AASN312
ATHR334
ALEU335
AGLN336
ALEU352
AGLY353
AMET354
AHIS355
AGLY374
AALA375
AARG376
AASP378
AARG380
AVAL381
AGLU407
AVAL408
AASN412
AGLY425
AASP426
AALA427
AHOH817
AHOH829
AHOH914
AHOH938
BPHE201

site_idAC8
Number of Residues5
Detailsbinding site for residue K B 701
ChainResidue
BGLN343
BASP350
BGLN506
BTRP508
BHOH825

site_idAC9
Number of Residues5
Detailsbinding site for residue MG B 702
ChainResidue
BASP550
BASN577
BHTL703
BHOH808
BHOH864

site_idAD1
Number of Residues21
Detailsbinding site for residue HTL B 703
ChainResidue
BGLY523
BMET525
BGLY549
BASP550
BALA551
BSER552
BASN577
BMG702
BOXY704
BOXY708
BHOH808
ATYR113
APRO114
AGLU139
APRO165
AASN169
AGLN202
ACO2706
BVAL497
BGLN499
BHIS500

site_idAD2
Number of Residues3
Detailsbinding site for residue OXY B 704
ChainResidue
ACO2706
BMET582
BHTL703

site_idAD3
Number of Residues4
Detailsbinding site for residue OXY B 705
ChainResidue
BGLU578
BGLN580
BHIS599
BGLN600

site_idAD4
Number of Residues3
Detailsbinding site for residue OXY B 706
ChainResidue
AGLN600
BTYR113
BHOH885

site_idAD5
Number of Residues4
Detailsbinding site for residue OXY B 707
ChainResidue
BGLU578
BGLN600
BLEU601
BASN602

site_idAD6
Number of Residues4
Detailsbinding site for residue OXY B 708
ChainResidue
BGLN499
BMET582
BHTL703
BHOH864

site_idAD7
Number of Residues7
Detailsbinding site for residue OXY B 709
ChainResidue
BGLY115
BGLY116
BALA117
BTHR162
BSER163
BGLN202
BACT712

site_idAD8
Number of Residues5
Detailsbinding site for residue PO4 B 710
ChainResidue
AHIS126
BGLU541
BHIS597
BTHR598
BHIS599

site_idAD9
Number of Residues31
Detailsbinding site for residue FAD B 711
ChainResidue
APHE201
BARG241
BGLY307
BALA308
BGLY309
BASN312
BTHR334
BLEU335
BLEU352
BMET354
BHIS355
BGLY374
BALA375
BARG376
BASP378
BARG380
BVAL381
BGLU407
BVAL408
BASN412
BGLY425
BASP426
BALA427
BGLN501
BMET502
BGLY520
BGLY521
BHOH820
BHOH844
BHOH852
BHOH876

site_idAE1
Number of Residues5
Detailsbinding site for residue ACT B 712
ChainResidue
ATPP703
BGLY116
BGLN202
BOXY709
BHOH847

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_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 2024-07-17

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