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1VLC

Crystal structure of 3-isopropylmalate dehydrogenase (TM0556) from Thermotoga maritima at 1.90 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003862molecular_function3-isopropylmalate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009098biological_processL-leucine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 355
ChainResidue
AGLY139
AVAL140
AMET240

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NMFGDIlSDesAalp.GSLGL
ChainResidueDetails
AASN239-LEU258

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY74
AARG95
AARG105
AARG134
AASP219
AASP243
AASP247
AGLY275

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Important for catalysis => ECO:0000250
ChainResidueDetails
ATYR141
ALYS187

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ATYR141

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ALYS187
AASP219

223166

PDB entries from 2024-07-31

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