Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6BD9

Saccharomyces cerevisiae acetohydroxyacid synthase

Replaces:  5INU
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
AGLN506
ATRP508
AHOH836
AHOH970
AHOH1078

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 702
ChainResidue
AHOH864
AHOH1013
AASP550
AASN577
ATPP704

site_idAC3
Number of Residues28
Detailsbinding site for residue FAD A 703
ChainResidue
AARG241
AGLY307
AALA308
AGLY309
AASN312
ATHR334
ALEU335
ALEU352
AGLY353
AMET354
AHIS355
AGLY356
AGLY374
AALA375
AARG376
AASP378
AARG380
AVAL381
AGLU407
AVAL408
AASN412
AGLY425
AASP426
AALA427
AHOH883
AHOH919
AHOH950
AHOH1021

site_idAC4
Number of Residues26
Detailsbinding site for residue TPP A 704
ChainResidue
AVAL497
AGLY498
AGLN499
AHIS500
AGLY523
AMET525
AGLY549
AASP550
AALA551
ASER552
AASN577
AMG702
AHOH864
AHOH895
AHOH907
AHOH1013
AHOH1045
BTYR113
BPRO114
BGLY115
BGLU139
BPRO165
BASN169
BGLN202
BPYR705
BOXY711

site_idAC5
Number of Residues8
Detailsbinding site for residue PYR A 705
ChainResidue
AGLY115
AGLY116
APHE201
AGLN202
APYR706
AOXY708
BTPP704
BOXY712

site_idAC6
Number of Residues8
Detailsbinding site for residue PYR A 706
ChainResidue
AGLY116
AALA117
ASER163
APHE201
AGLN202
ALYS251
APYR705
AOXY708

site_idAC7
Number of Residues6
Detailsbinding site for residue OXY A 707
ChainResidue
AALA551
AGLN600
AHOH801
AHOH819
BTYR113
BLYS137

site_idAC8
Number of Residues8
Detailsbinding site for residue OXY A 708
ChainResidue
AGLY115
AGLY116
AALA117
ATHR162
ASER163
AGLN202
APYR705
APYR706

site_idAC9
Number of Residues6
Detailsbinding site for residue K B 701
ChainResidue
BHOH884
BHOH937
BGLN343
BGLN506
BTRP508
BHOH801

site_idAD1
Number of Residues31
Detailsbinding site for residue FAD B 702
ChainResidue
APHE201
BARG241
BGLY307
BALA308
BGLY309
BASN312
BTHR334
BLEU335
BLEU352
BMET354
BHIS355
BGLY374
BALA375
BARG376
BARG380
BVAL381
BGLU407
BVAL408
BSER409
BASN412
BGLY425
BASP426
BALA427
BGLN501
BMET502
BGLY520
BGLY521
BHOH896
BHOH916
BHOH926
BHOH962

site_idAD2
Number of Residues5
Detailsbinding site for residue MG B 703
ChainResidue
BASP550
BASN577
BTPP704
BHOH877
BHOH981

site_idAD3
Number of Residues24
Detailsbinding site for residue TPP B 704
ChainResidue
ATYR113
APRO114
AGLY115
AGLU139
APRO165
AASN169
APYR705
BVAL497
BGLY498
BGLN499
BHIS500
BGLY523
BMET525
BGLY549
BASP550
BALA551
BSER552
BASN577
BMG703
BOXY712
BHOH866
BHOH877
BHOH964
BHOH981

site_idAD4
Number of Residues9
Detailsbinding site for residue PYR B 705
ChainResidue
ATPP704
AHOH895
BGLY116
BPHE201
BGLN202
BPYR706
BOXY710
BOXY711
BHOH835

site_idAD5
Number of Residues6
Detailsbinding site for residue PYR B 706
ChainResidue
BGLY116
BALA117
BSER163
BPYR705
BOXY710
BHOH878

site_idAD6
Number of Residues4
Detailsbinding site for residue OXY B 707
ChainResidue
BGLU578
BGLN580
BHIS599
BGLN600

site_idAD7
Number of Residues5
Detailsbinding site for residue OXY B 708
ChainResidue
BGLU578
BGLN600
BLEU601
BASN602
BHOH821

site_idAD8
Number of Residues2
Detailsbinding site for residue OXY B 709
ChainResidue
AHOH1045
BTYR113

site_idAD9
Number of Residues7
Detailsbinding site for residue OXY B 710
ChainResidue
BGLY116
BALA117
BTHR162
BSER163
BGLN202
BPYR705
BPYR706

site_idAE1
Number of Residues4
Detailsbinding site for residue OXY B 711
ChainResidue
ATPP704
BGLY115
BPYR705
BHOH843

site_idAE2
Number of Residues3
Detailsbinding site for residue OXY B 712
ChainResidue
APYR705
BMET582
BTPP704

site_idAE3
Number of Residues6
Detailsbinding site for residue PO4 B 713
ChainResidue
AHIS126
BGLU541
BHIS597
BTHR598
BHIS599
BHOH967

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

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon