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5D6R

Acetolactate Synthase from Klebsiella pneumoniae in Complex with Mechanism-Based Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
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
M0000287molecular_functionmagnesium ion binding
M0003824molecular_functioncatalytic activity
M0003984molecular_functionacetolactate synthase activity
M0016740molecular_functiontransferase activity
M0019752biological_processcarboxylic acid metabolic process
M0030976molecular_functionthiamine pyrophosphate binding
M0034077biological_processbutanediol metabolic process
M0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG B 601
ChainResidue
BASP447
BASP474
BGLY476
BEN0605
BHOH705

site_idAC2
Number of Residues4
Detailsbinding site for residue MG B 602
ChainResidue
BSER129
BTHR132
BHOH776
BHOH816

site_idAC3
Number of Residues5
Detailsbinding site for residue MG B 603
ChainResidue
BARG69
BGLN220
BPRO221
BHOH747
BHOH784

site_idAC4
Number of Residues10
Detailsbinding site for residue PO4 B 604
ChainResidue
BPHE256
BGLY258
BARG259
BGLN266
BARG352
BALA402
BARG403
BLEU405
BTYR406
BHOH708

site_idAC5
Number of Residues27
Detailsbinding site for residue EN0 B 605
ChainResidue
BPRO33
BALA35
BGLU57
BPRO83
BASN87
BGLN120
BMET394
BGLY395
BSER396
BPHE397
BGLN420
BMET422
BGLY446
BASP447
BGLY448
BGLY449
BASP474
BGLY476
BTYR477
BASN478
BMET479
BVAL480
BTYR543
BMG601
BHOH705
BHOH715
BHOH761

site_idAC6
Number of Residues5
Detailsbinding site for residue MG M 601
ChainResidue
MASP447
MASP474
MGLY476
MEN0604
MHOH708

site_idAC7
Number of Residues4
Detailsbinding site for residue MG M 602
ChainResidue
MSER129
MTHR132
MHOH733
MHOH833

site_idAC8
Number of Residues7
Detailsbinding site for residue PO4 M 603
ChainResidue
MGLY258
MARG259
MGLN266
MARG352
MLEU405
MTYR406
MHOH711

site_idAC9
Number of Residues26
Detailsbinding site for residue EN0 M 604
ChainResidue
MPRO33
MALA35
MGLU57
MTHR80
MASN87
MMET394
MGLY395
MSER396
MPHE397
MGLN420
MMET422
MGLY446
MASP447
MGLY448
MGLY449
MASP474
MGLY476
MTYR477
MASN478
MMET479
MVAL480
MGLN483
MTYR543
MMG601
MHOH708
MHOH731

Functional Information from PROSITE/UniProt
site_idPS00187
Number of Residues20
DetailsTPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGawlvnPerkvVsVsGDGG
ChainResidueDetails
BILE430-GLY449

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BARG159
BPHE263
BASP304
BASP447
MARG159
MPHE263
MASP304
MASP447

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 722
ChainResidueDetails
BMET394electrostatic stabiliser
BMET422steric role
BASP447metal ligand
BASP474metal ligand
BGLY476metal ligand

site_idMCSA2
Number of Residues5
DetailsM-CSA 722
ChainResidueDetails
MMET394electrostatic stabiliser
MMET422steric role
MASP447metal ligand
MASP474metal ligand
MGLY476metal ligand

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PDB entries from 2024-07-17

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