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4XXV

Crystal structure of 3-isopropylmalate dehydrogenase from Burkholderia thailandensis in complex with 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
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0000287molecular_functionmagnesium ion binding
B0003862molecular_function3-isopropylmalate dehydrogenase activity
B0005737cellular_componentcytoplasm
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 Residues29
Detailsbinding site for residue NAD B 400
ChainResidue
AASN192
BGLU83
BILE259
BGLU276
BHIS279
BGLY280
BSER281
BALA282
BPRO283
BASP284
BILE285
ATYR220
BALA291
BASN292
BGOL401
BHOH587
BHOH612
BHOH623
BHOH640
BHOH679
BHOH723
BHOH949
AASN223
AHOH546
AHOH556
BILE11
BALA67
BVAL68
BGLY69

site_idAC2
Number of Residues10
Detailsbinding site for residue GOL B 401
ChainResidue
ALYS190
BARG90
BARG100
BARG128
BTYR135
BASP246
BSER278
BNAD400
BHOH654
BHOH957

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL B 402
ChainResidue
BPHE99
BTYR306
BHOH631
BHOH890

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NMFGDIlSDeaSmlt.GSIGM
ChainResidueDetails
AASN242-MET261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01033
ChainResidueDetails
AARG90
BARG128
BASP222
BASP246
BASP250
BGLY280
AARG100
AARG128
AASP222
AASP246
AASP250
AGLY280
BARG90
BARG100

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Important for catalysis => ECO:0000255|HAMAP-Rule:MF_01033
ChainResidueDetails
ATYR135
ALYS190
BTYR135
BLYS190

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PDB entries from 2024-07-10

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