Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1IDM

3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003862molecular_function3-isopropylmalate dehydrogenase activity
A0009098biological_processL-leucine biosynthetic process
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NIFGDIlSDlaSvlp.GSLGL
ChainResidueDetails
AASN235-LEU254

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:7881901
ChainResidueDetails
AGLY74
APRO275

site_idSWS_FT_FI2
Number of Residues13
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER94
ATHR133
AALA218
ASER242
ASER246
AALA104
ALEU132
AMET217
ALEU241
AALA245
AALA274
AGLN95
ALYS105

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Important for catalysis => ECO:0000250
ChainResidueDetails
AGLY139
AASN185
AVAL186

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for catalysis
ChainResidueDetails
AGLU140

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ATYR137

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
AASP215
ALYS183

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon