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5ZI4

MDH3 wild type, nad-oaa-form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003729molecular_functionmRNA binding
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0006108biological_processmalate metabolic process
A0006635biological_processfatty acid beta-oxidation
A0006735biological_processNADH regeneration
A0016491molecular_functionoxidoreductase activity
A0016615molecular_functionmalate dehydrogenase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
A0030060molecular_functionL-malate dehydrogenase (NAD+) activity
B0003729molecular_functionmRNA binding
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0005782cellular_componentperoxisomal matrix
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0006108biological_processmalate metabolic process
B0006635biological_processfatty acid beta-oxidation
B0006735biological_processNADH regeneration
B0016491molecular_functionoxidoreductase activity
B0016615molecular_functionmalate dehydrogenase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
B0030060molecular_functionL-malate dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue OAA A 401
ChainResidue
AARG80
AASN118
AARG152
AHIS187
AGLY220
AALA233
ANAD402
AHOH511
AHOH529

site_idAC2
Number of Residues31
Detailsbinding site for residue NAD A 402
ChainResidue
AGLY8
ASER10
AGLY11
AGLY12
AVAL13
ATYR33
AASP34
AILE35
APRO75
AALA76
AGLY77
AVAL78
APRO79
AASN93
AILE96
ALEU100
AILE116
AASN118
AVAL145
AHIS187
AALA233
AMET237
AOAA401
AHOH508
AHOH509
AHOH511
AHOH516
AHOH524
AHOH535
AHOH539
AHOH549

site_idAC3
Number of Residues10
Detailsbinding site for residue OAA B 401
ChainResidue
BARG80
BASN118
BARG152
BHIS187
BGLY220
BALA233
BNAD402
BHOH536
BHOH539
BHOH554

site_idAC4
Number of Residues34
Detailsbinding site for residue NAD B 402
ChainResidue
BGLY8
BSER10
BGLY11
BGLY12
BVAL13
BTYR33
BASP34
BILE35
BPRO75
BALA76
BGLY77
BVAL78
BPRO79
BASN93
BLEU100
BILE116
BASN118
BVAL145
BHIS187
BALA233
BTHR234
BMET237
BOAA401
BHOH509
BHOH513
BHOH514
BHOH520
BHOH522
BHOH523
BHOH534
BHOH536
BHOH546
BHOH559
BHOH575

Functional Information from PROSITE/UniProt
site_idPS00068
Number of Residues13
DetailsMDH Malate dehydrogenase active site signature. VTNLDlvRAetfL
ChainResidueDetails
AVAL145-LEU157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00346
ChainResidueDetails
AHIS187
BHIS187

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P40926
ChainResidueDetails
AGLY8
BMET237
AASP34
AASN93
AILE116
AMET237
BGLY8
BASP34
BASN93
BILE116

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10004
ChainResidueDetails
AARG80
AARG86
AASN118
AARG152
BARG80
BARG86
BASN118
BARG152

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PDB entries from 2024-07-24

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