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1IPD

THREE-DIMENSIONAL STRUCTURE OF A HIGHLY THERMOSTABLE ENZYME, 3-ISOPROPYLMALATE DEHYDROGENASE OF THERMUS THERMOPHILUS AT 2.2 ANGSTROMS RESOLUTION

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 346
ChainResidue
APRO13
AGLU17
AARG167
AGLU201
AVAL202
AGLY205

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 347
ChainResidue
AASP47
ALYS178
AASP208

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 Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:7881901
ChainResidueDetails
AGLY74
AGLY274

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG94
AARG104
AARG132
AASP217
AASP241
AASP245

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for catalysis
ChainResidueDetails
ATYR139

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for catalysis => ECO:0000250
ChainResidueDetails
ALYS185

218853

PDB entries from 2024-04-24

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