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2Y3Z

Structure of Isopropylmalate dehydrogenase from Thermus thermophilus - apo enzyme

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
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 TRS A 1351
ChainResidue
AARG104
AASP217
AASP241
AASP245
AHOH2115
AHOH2142
AHOH2143
AHOH2198

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 2PE A 1352
ChainResidue
AALA172
ALYS175
AASP278
AALA280
AHIS300
AALA301
APHE302
AGLY303
AHOH2200
AGLU171

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 2PE A 1353
ChainResidue
AARG94
AASN102
AARG104
AARG132
APHE140
AVAL188
ASER259
AGLU270
AGOL1357
AHOH2142

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 2PE A 1354
ChainResidue
AVAL72
AGLY73
AGLY74
ALEU254
AHIS273
AGLY274
ASER275
AALA276
APRO277
AALA285
AASN286
AGOL1357
AHOH2199
AHOH2201

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1355
ChainResidue
ALYS76
AGLY303
AVAL305
AHOH2200

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1356
ChainResidue
AGLU212
AGLN214
AARG229

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 1357
ChainResidue
ASER71
AVAL72
AGLU270
APRO271
AVAL272
AHIS273
AGLY274
A2PE1353
A2PE1354
AHOH2039
AHOH2201

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

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PDB entries from 2024-11-06

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