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1IVH

STRUCTURE OF HUMAN ISOVALERYL-COA DEHYDROGENASE AT 2.6 ANGSTROMS RESOLUTION: STRUCTURAL BASIS FOR SUBSTRATE SPECIFICITY

Functional Information from GO Data
ChainGOidnamespacecontents
A0003995molecular_functionacyl-CoA dehydrogenase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006552biological_processL-leucine catabolic process
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0008470molecular_function3-methylbutanoyl-CoA dehydrogenase activity
A0009083biological_processbranched-chain amino acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
A0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
A0042802molecular_functionidentical protein binding
A0050660molecular_functionflavin adenine dinucleotide binding
B0003995molecular_functionacyl-CoA dehydrogenase activity
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006552biological_processL-leucine catabolic process
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0008470molecular_function3-methylbutanoyl-CoA dehydrogenase activity
B0009083biological_processbranched-chain amino acid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
B0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
B0042802molecular_functionidentical protein binding
B0050660molecular_functionflavin adenine dinucleotide binding
C0003995molecular_functionacyl-CoA dehydrogenase activity
C0005515molecular_functionprotein binding
C0005654cellular_componentnucleoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0006552biological_processL-leucine catabolic process
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0008470molecular_function3-methylbutanoyl-CoA dehydrogenase activity
C0009083biological_processbranched-chain amino acid catabolic process
C0016491molecular_functionoxidoreductase activity
C0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
C0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
C0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
C0042802molecular_functionidentical protein binding
C0050660molecular_functionflavin adenine dinucleotide binding
D0003995molecular_functionacyl-CoA dehydrogenase activity
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0006552biological_processL-leucine catabolic process
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0008470molecular_function3-methylbutanoyl-CoA dehydrogenase activity
D0009083biological_processbranched-chain amino acid catabolic process
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0016937molecular_functionshort-chain fatty acyl-CoA dehydrogenase activity
D0033539biological_processfatty acid beta-oxidation using acyl-CoA dehydrogenase
D0042802molecular_functionidentical protein binding
D0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD A 399
ChainResidue
ALEU133
AGLU379
ALEU383
ACOS400
AHOH512
AHOH589
BARG280
BPHE283
BILE287
BPHE290
BMET293
AMET135
BGLN348
BCYS349
BGLY352
DGLN291
ASER136
AGLY141
ASER142
ATRP166
ATHR168
AILE373
ATHR377

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE COS A 400
ChainResidue
AGLY141
ASER142
AVAL144
ASER190
AARG191
AVAL244
ATYR245
AMET248
AASP252
AGLU254
AARG255
AALA375
AGLY376
AVAL380
AVAL384
AARG387
AFAD399
BPHE283

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD B 399
ChainResidue
AARG280
APHE283
APHE290
AMET293
AGLN348
ACYS349
AGLY352
BLEU133
BMET135
BSER136
BGLY141
BSER142
BTRP166
BILE167
BTHR168
BLEU370
BILE373
BTHR377
BGLU379
BCOS400
BHOH525
BHOH531
BHOH591
CGLN291

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE COS B 400
ChainResidue
APHE283
BGLY141
BSER142
BVAL144
BVAL145
BSER190
BARG191
BVAL244
BTYR245
BMET248
BLEU251
BASP252
BGLU254
BARG255
BGLY374
BALA375
BGLY376
BVAL380
BARG387
BFAD399
BHOH545

site_idAC5
Number of Residues28
DetailsBINDING SITE FOR RESIDUE FAD C 399
ChainResidue
CLEU383
CCOS400
CHOH500
CHOH505
CHOH517
CHOH547
CHOH587
DARG280
DPHE283
DILE287
DPHE290
DMET293
DGLN348
DCYS349
DGLY352
BGLN291
CLEU133
CMET135
CSER136
CGLY141
CSER142
CTRP166
CILE167
CTHR168
CLEU370
CILE373
CTHR377
CGLU379

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE COS C 400
ChainResidue
CMET135
CGLY141
CSER142
CVAL144
CVAL145
CSER190
CARG191
CVAL244
CTYR245
CMET248
CLEU251
CGLU254
CARG255
CALA375
CGLY376
CVAL380
CARG387
CFAD399
CHOH587
CHOH686
DPHE283

site_idAC7
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FAD D 399
ChainResidue
AGLN291
CARG280
CILE287
CPHE290
CMET293
CGLN348
CCYS349
CGLY352
CHOH529
DLEU133
DMET135
DSER136
DGLY141
DSER142
DTRP166
DILE167
DTHR168
DLYS213
DLEU370
DILE373
DTHR377
DGLU379
DCOS400
DHOH564
DHOH605
DHOH655

site_idAC8
Number of Residues17
DetailsBINDING SITE FOR RESIDUE COS D 400
ChainResidue
CPHE283
DMET135
DGLY141
DSER142
DSER190
DVAL244
DMET248
DLEU251
DGLU254
DARG255
DGLY374
DALA375
DGLY376
DVAL380
DVAL384
DARG387
DFAD399

Functional Information from PROSITE/UniProt
site_idPS00072
Number of Residues13
DetailsACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. AMSEpnAGSDvvS
ChainResidueDetails
AALA134-SER146

site_idPS00073
Number of Residues20
DetailsACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QcFGGnGYinDfpmgRflrD
ChainResidueDetails
AGLN348-ASP367

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"7640268","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IVH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues104
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9214289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IVH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9JHI5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9JHI5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JHI5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 14728676, 9214289
ChainResidueDetails
AGLU254

site_idMCSA1
Number of Residues4
DetailsM-CSA 68
ChainResidueDetails
AALA132electrostatic stabiliser, hydrogen bond donor
ALEU133electrostatic stabiliser, hydrogen bond donor
ALEU251hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role
AVAL384electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 68
ChainResidueDetails
BALA132electrostatic stabiliser, hydrogen bond donor
BLEU133electrostatic stabiliser, hydrogen bond donor
BLEU251hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role
BVAL384electrostatic stabiliser

site_idMCSA3
Number of Residues4
DetailsM-CSA 68
ChainResidueDetails
CALA132electrostatic stabiliser, hydrogen bond donor
CLEU133electrostatic stabiliser, hydrogen bond donor
CLEU251hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role
CVAL384electrostatic stabiliser

site_idMCSA4
Number of Residues4
DetailsM-CSA 68
ChainResidueDetails
DALA132electrostatic stabiliser, hydrogen bond donor
DLEU133electrostatic stabiliser, hydrogen bond donor
DLEU251hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role
DVAL384electrostatic stabiliser

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PDB entries from 2025-10-15

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