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5WDG

Acetolactate Synthase from Klebsiella pneumoniae in Complex with a Reaction Intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0003984molecular_functionacetolactate synthase activity
A0016740molecular_functiontransferase activity
A0019752biological_processcarboxylic acid metabolic process
A0030976molecular_functionthiamine pyrophosphate binding
A0034077biological_processbutanediol metabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0003984molecular_functionacetolactate synthase activity
B0016740molecular_functiontransferase activity
B0019752biological_processcarboxylic acid metabolic process
B0030976molecular_functionthiamine pyrophosphate binding
B0034077biological_processbutanediol metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 601
ChainResidue
AASP447
AASP474
AGLY476
AA4Y605
AHOH729

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 602
ChainResidue
AHOH868
AARG69
AGLN220
AHOH810
AHOH842

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 603
ChainResidue
ASER129
ATHR132
AHOH804
AHOH833
AHOH882
AHOH890

site_idAC4
Number of Residues8
Detailsbinding site for residue PO4 A 604
ChainResidue
APHE256
AGLY258
AARG259
AGLN266
AARG352
AALA402
ALEU405
ATYR406

site_idAC5
Number of Residues24
Detailsbinding site for residue A4Y A 605
ChainResidue
APRO33
AGLY34
AALA35
AGLU57
AASN87
AMET394
ASER396
APHE397
AGLN420
AMET422
AGLY446
AASP447
AGLY448
AGLY449
AASP474
AGLY476
ATYR477
AASN478
AMET479
AVAL480
ATYR543
AMG601
AHOH729
AHOH807

site_idAC6
Number of Residues8
Detailsbinding site for residue PYR A 606
ChainResidue
ASER97
AGLY99
AARG159
APRO160
ALEU216
AGLN243
AVAL286
AHOH771

site_idAC7
Number of Residues5
Detailsbinding site for residue MG B 601
ChainResidue
BASP447
BASP474
BGLY476
BA4Y605
BHOH765

site_idAC8
Number of Residues5
Detailsbinding site for residue MG B 602
ChainResidue
BSER129
BTHR132
BHOH834
BHOH899
BHOH950

site_idAC9
Number of Residues5
Detailsbinding site for residue MG B 603
ChainResidue
BLEU44
BSER47
BILE49
BHOH896
BHOH923

site_idAD1
Number of Residues7
Detailsbinding site for residue PO4 B 604
ChainResidue
BGLY258
BARG259
BGLN266
BARG352
BTYR406
BHOH744
BHOH778

site_idAD2
Number of Residues28
Detailsbinding site for residue A4Y B 605
ChainResidue
BTYR543
BMG601
BHOH741
BHOH742
BHOH762
BHOH765
BHOH775
BPRO33
BGLY34
BALA35
BGLU57
BASN87
BMET394
BGLY395
BSER396
BPHE397
BGLN420
BMET422
BGLY446
BASP447
BGLY448
BGLY449
BASP474
BGLY476
BTYR477
BASN478
BMET479
BVAL480

site_idAD3
Number of Residues7
Detailsbinding site for residue PYR B 606
ChainResidue
AARG544
AASP545
BTYR488
BGLN489
BARG490
BHOH810
BHOH814

Functional Information from PROSITE/UniProt
site_idPS00187
Number of Residues20
DetailsTPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGawlvnPerkvVsVsGDGG
ChainResidueDetails
AILE430-GLY449

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG159
APHE263
AASP304
AASP447
BARG159
BPHE263
BASP304
BASP447

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 722
ChainResidueDetails
AMET394electrostatic stabiliser
AMET422steric role
AASP447metal ligand
AASP474metal ligand
AGLY476metal ligand

site_idMCSA2
Number of Residues5
DetailsM-CSA 722
ChainResidueDetails
BMET394electrostatic stabiliser
BMET422steric role
BASP447metal ligand
BASP474metal ligand
BGLY476metal ligand

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PDB entries from 2024-07-10

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