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2Y41

Structure of Isopropylmalate dehydrogenase from Thermus thermophilus - complex with IPM and MN

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003862molecular_function3-isopropylmalate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009082biological_processbranched-chain amino acid biosynthetic process
A0009098biological_processL-leucine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0000287molecular_functionmagnesium ion binding
B0003862molecular_function3-isopropylmalate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0009082biological_processbranched-chain amino acid biosynthetic process
B0009098biological_processL-leucine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IPM A 800
ChainResidue
AARG94
BVAL188
BASP217
AARG104
AARG132
ATYR139
AASP241
AMN999
AHOH2116
AHOH2117
BLYS185

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 999
ChainResidue
AASP241
AIPM800
AHOH2118
AHOH2119
BLYS185
BASP217

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE IPM B 800
ChainResidue
ALYS185
AVAL188
AASP217
BARG94
BARG104
BARG132
BTYR139
BASP241
BMN999
BHOH2078
BHOH2080
BHOH2081

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 999
ChainResidue
AASP217
BASP241
BASP245
BIPM800
BHOH2080
BHOH2081

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B 1000
ChainResidue
BHOH2082
BHOH2082
BHOH2083
BHOH2083
BHOH2084
BHOH2085
BHOH2085

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 1001
ChainResidue
BHOH2086
BHOH2087
BHOH2088
BHOH2089
BHOH2090

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NIFGDIlSDlaSvlp.GSLGL
ChainResidueDetails
AASN237-LEU256

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues50
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7881901","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Important for catalysis"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Important for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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