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4IWH

Crystal structure of a 3-isopropylmalate dehydrogenase from Burkholderia pseudomallei

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003862molecular_function3-isopropylmalate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009098biological_processL-leucine biosynthetic process
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
B0000287molecular_functionmagnesium ion binding
B0003862molecular_function3-isopropylmalate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009098biological_processL-leucine biosynthetic process
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP246
AASP250
AHOH660
AHOH733
BASP222
BHOH559

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
BASP250
BHOH672
BHOH757
BHOH759
AASP222
AHOH734
BASP246

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NMFGDIlSDeaSmlt.GSIGM
ChainResidueDetails
AASN242-MET261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01033","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsSite: {"description":"Important for catalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01033","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

254587

PDB entries from 2026-06-03

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