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2ZTW

Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003862molecular_function3-isopropylmalate dehydrogenase activity
A0005737cellular_componentcytoplasm
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 Residues8
DetailsBINDING SITE FOR RESIDUE NAD A 400
ChainResidue
AHIS273
AGLY274
AALA276
AASP278
AILE279
AALA285
AASN286
AHOH471

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DEI A 401
ChainResidue
ASER259
AGLU270
AVAL272
AASN102

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
APHE170
AGLY203
ATYR206
AVAL209

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

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ATYR139

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ALYS185
AASP217

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PDB entries from 2024-07-17

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