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1V16

CROSSTALK BETWEEN COFACTOR BINDING AND THE PHOSPHORYLATION LOOP CONFORMATION IN THE BCKD MACHINE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003863molecular_function3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0009083biological_processbranched-chain amino acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
A0016831molecular_functioncarboxy-lyase activity
A0046872molecular_functionmetal ion binding
A0047101molecular_functionbranched-chain alpha-keto acid dehydrogenase activity
A0120552
A0160157cellular_componentbranched-chain alpha-ketoacid dehydrogenase complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 501
ChainResidue
AGLN112
ASER161
APRO163
ATHR166
AGLN167
AHOH2099

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 503
ChainResidue
ATPP601
AHOH2306
AGLU193
AASN222
ATYR224

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 504
ChainResidue
ATYR113
ATPP601
BTYR102
BHIS146

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 505
ChainResidue
AHIS392
BTRP330

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 506
ChainResidue
AARG79

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 507
ChainResidue
ABEN701

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K B 502
ChainResidue
BGLY128
BLEU130
BTHR131
BCYS178
BASP181
BASN183
BHOH2145

site_idAC8
Number of Residues26
DetailsBINDING SITE FOR RESIDUE TPP A 601
ChainResidue
AARG114
ASER162
ALEU164
AGLY192
AGLU193
AGLY194
AALA195
AGLU198
AARG220
AASN222
ATYR224
AALA225
AILE226
AMN503
ACL504
AHOH2166
AHOH2306
AHOH2307
AHOH2308
AHOH2309
AHOH2310
BGLU46
BLEU74
BGLU76
BGLN98
BTYR102

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BEN A 701
ChainResidue
AILE73
AGLU76
AGLN80
AARG82
ACL507
AHOH2073

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 701
ChainResidue
AGLN374
BTRP260
BTHR284
BGLU290
BTHR294
BARG309
BHOH2258

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 702
ChainResidue
ALYS153
AARG185
BVAL88
BTHR89
BPHE125
BHOH2079
BHOH2112
BHOH2259

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 703
ChainResidue
BARG309
BCYS311
BTYR313
BHOH2260
BHOH2261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:10745006, ECO:0007744|PDB:1DTW
ChainResidueDetails
BTYR102
AALA195
AARG220
AASN222
ATYR224
AALA291
BGLY128
BLEU130
BTHR131
BCYS178
BASP181
BASN183
AGLU193
AGLY194

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q6P3A8
ChainResidueDetails
BLYS182

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS191

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P50136
ChainResidueDetails
ASER294
ASER302

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P50136
ChainResidueDetails
ALYS311

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P50136
ChainResidueDetails
ALYS335

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BGLU76

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BGLU76
BHIS146

site_idMCSA1
Number of Residues2
DetailsM-CSA 280
ChainResidueDetails
AGLU76activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role
ASER162hydrogen bond acceptor, steric role

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PDB entries from 2025-06-11

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