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6XXY

Crystal structure of Haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with O-isobutenyl oxalylhydroxamate.

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
B0000287molecular_functionmagnesium ion binding
B0003862molecular_function3-isopropylmalate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009098biological_processL-leucine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues31
Detailsbinding site for residue NAD A 401
ChainResidue
AILE14
AGLU280
AGLY283
AGLY284
ASER285
AALA286
APRO287
AASP288
AILE289
AASN296
AO45404
ASER74
AHOH518
AHOH540
AHOH542
AHOH562
AHOH570
AHOH620
AHOH637
BASN196
BTYR224
BASN227
AVAL75
BHOH562
BHOH563
AGLY76
AGLY77
AGLU90
ALEU94
AMET263
AGLY264

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 402
ChainResidue
AARG108
AASP250
ASER253
AASP254
AO45404
BASP226

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 403
ChainResidue
AASP226
BASP250
BASP254
BO45402
BHOH509
BHOH511

site_idAC4
Number of Residues11
Detailsbinding site for residue O45 A 404
ChainResidue
AGLU90
AARG98
AARG108
AARG137
AASP250
AALA282
ANAD401
AMG402
AHOH541
BLYS194
BASP226

site_idAC5
Number of Residues31
Detailsbinding site for residue NAD B 401
ChainResidue
AASN196
ATYR224
AASN227
AHOH593
BILE14
BSER74
BVAL75
BGLY76
BGLY77
BGLU90
BLEU94
BMET263
BGLY264
BGLU280
BGLY283
BGLY284
BSER285
BALA286
BPRO287
BASP288
BILE289
BASN296
BASP337
BO45402
BHOH508
BHOH512
BHOH525
BHOH527
BHOH532
BHOH554
BHOH582

site_idAC6
Number of Residues15
Detailsbinding site for residue O45 B 402
ChainResidue
BHOH511
ALYS194
AASN196
AASP226
AMG403
BGLU90
BLEU95
BARG98
BARG108
BARG137
BASP250
BALA282
BNAD401
BHOH507
BHOH509

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NIFGDIiSDeaAmit.GSMGM
ChainResidueDetails
AASN246-MET265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY77
BARG98
BARG108
BARG137
BASP226
BASP250
BASP254
BGLY284
AARG98
AARG108
AARG137
AASP226
AASP250
AASP254
AGLY284
BGLY77

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Important for catalysis => ECO:0000250
ChainResidueDetails
ATYR144
ALYS194
BTYR144
BLYS194

220113

PDB entries from 2024-05-22

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