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1UMC

branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8 with 4-methylpentanoate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003863molecular_function3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity
A0005515molecular_functionprotein binding
A0016491molecular_functionoxidoreductase activity
A0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0003863molecular_function3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity
B0005515molecular_functionprotein binding
B0016491molecular_functionoxidoreductase activity
C0003863molecular_function3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity
C0005515molecular_functionprotein binding
C0016491molecular_functionoxidoreductase activity
C0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0003863molecular_function3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity
D0005515molecular_functionprotein binding
D0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1401
ChainResidue
AASP175
AASN204
ATYR206
ATPP1402
AHOH1428

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 2401
ChainResidue
CHOH2430
CASP175
CASN204
CTYR206
CTPP2402

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE TPP A 1402
ChainResidue
ATYR94
ATYR95
AARG96
ASER144
APRO145
AILE146
AGLY174
AASP175
AGLY176
AALA177
AGLU180
AASN204
ATYR206
AALA207
AILE208
AHIS273
AMG1401
AHOH1405
AHOH1410
AHOH1428
DGLU29
DLEU58
DGLU60
DGLN82
DTYR86
D4MV1403

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 4MV D 1403
ChainResidue
ATYR95
AMET128
AHIS131
ATPP1402
AHOH1575
DPHE83
DTYR86
DHIS128
DHOH1520

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE TPP C 2402
ChainResidue
BGLU29
BLEU58
BGLU60
BGLN82
BTYR86
CTYR94
CTYR95
CARG96
CSER144
CPRO145
CILE146
CGLY174
CASP175
CGLY176
CALA177
CGLU180
CASN204
CTYR206
CALA207
CILE208
CHIS273
CMG2401
CHOH2405
CHOH2422
CHOH2430

Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. KEEL
ChainResidueDetails
ALYS364-LEU367

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
BHIS129
AHIS273
CPHE66
CTYR94
CTYR95
CMET128
CSER144
CGLY174
CASP175
CASN204
CTYR206
DHIS129
CHIS273
ATYR95
AMET128
ASER144
AGLY174
AASP175
AASN204
ATYR206

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15033367
ChainResidueDetails
BGLU29
BGLN82
DGLU29
DGLN82

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
BLEU58
BPHE83
BTYR86
DLEU58
DPHE83
DTYR86

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
BHIS129
DHIS129

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
CHIS273
BGLU60
BHIS129

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
AHIS273
DGLU60
DHIS129

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PDB entries from 2024-07-17

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