_EC 1.1.1.37 Malate dehydrogenase. 68 PDB entries  
EC 1.-.-.- Oxidoreductases. [9,379 PDB entries]
EC 1.1.-.- Acting on the CH-OH group of donors. [2,048 PDB entries]
EC 1.1.1.- With NAD(+) or NADP(+) as acceptor. [1,830 PDB entries]
EC 1.1.1.37 Malate dehydrogenase. [68 PDB entries]    
1b8p

Pathway: Citric acid cycle
Reaction: (S)-malate + NAD(+) = oxaloacetate + Nadh.
 


(S)-malate
+
NAD(+)
=
oxaloacetate
+
NADH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Malic dehydrogenase.
Comments: Also oxidizes some other 2-hydroxydicarboxylic acids.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 68 PDB entries in enzyme class E.C.1.1.1.37

  PDB code Protein
1b8p
Malate dehydrogenase from aquaspirillum arcticum
Source: Aquaspirillum arcticum. Organism_taxid: 87645
Chain: A (327 residues) CATH domains: 3.40.50.720 3.90.110.10
1b8u
Malate dehydrogenase from aquaspirillum arcticum
Source: Aquaspirillum arcticum. Organism_taxid: 87645
Chain: A (327 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group OAA corresponds to enzyme reactant (S)-malate
  Het Group NAD corresponds to enzyme reactant NAD(+)
1b8v
Malate dehydrogenase from aquaspirillum arcticum
Source: Aquaspirillum arcticum. Organism_taxid: 87645
Chain: A (327 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1bdm
The structure at 1.8 angstroms resolution of a single site mutant (t189i) of malate dehydrogenase from thermus flavus with increased enzymatic activity
Source: Thermus thermophilus. Organism_taxid: 274.
Chains: A, B (318 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAX is 97.00% similar to enzyme reactant NAD(+)
1bmd
Determinants of protein thermostability observed in the 1.9 angstroms crystal structure of malate dehydrogenase from the thermophilic bacterium thermus flavus
Source: Thermus thermophilus. Organism_taxid: 274.
Chains: A, B (327 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1d3a
Crystal structure of the wild type halophilic malate dehydro the apo form
Source: Haloarcula marismortui. Organism_taxid: 2238. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (303 residues) CATH domains: 3.90.110.10 3.40.50.720
1emd
Crystal structure of a ternary complex of escherichia coli m dehydrogenase, citrate and NAD at 1.9 angstroms resolution
Source: Escherichia coli. Organism_taxid: 562
Chain: A (312 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group CIT is 69.23% similar to enzyme reactant (S)-malate
  Het Group NAD corresponds to enzyme reactant NAD(+)
1gt2
R207s,r292s mutant of malate dehydrogenase from the halophilic archaeon haloarcula marismortui (holo form)
Source: Haloarcula marismortui. Organism_taxid: 2238. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (303 residues) CATH domains: 3.90.110.10 3.40.50.720
Bound ligand:   Het Group NAD corresponds to enzyme product NADH
1guy
Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases
Source: Chloroflexus aurantiacus. Organism_taxid: 1108. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, C (296 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1guz
Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases
Source: Chlorobium vibrioforme, chlorobium tepidum. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: hybrid between mdh from chlorobium vibrioforme and chlorobium tepidum
Chains: A, B, C, D (305 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1gv0
Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases
Source: Chlorobium tepidum. Organism_taxid: 1097. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (301 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1gv1
Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases
Source: Chlorobium vibrioforme. Organism_taxid: 1098. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (305 residues) CATH domains: 3.40.50.720 3.90.110.10
1hlp
Structural features stabilizing halophilic malate dehydrogenase from an archaebacterium
Source: Haloarcula marismortui. Organism_taxid: 2238. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (303 residues) CATH domains: 3.90.110.10 3.40.50.720
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1hye
Crystal structure of the mj0490 gene product, the family of lactate/malate dehydrogenase, dimeric structure
Source: Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: mj0490. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (307 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAP is 91.00% similar to enzyme reactant NAD(+)
1hyg
Crystal structure of mj0490 gene product, the family of lactate/malate dehydrogenase
Source: Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: mj0490. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (313 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAP is 91.00% similar to enzyme reactant NAD(+)
1ib6
Crystal structure of r153c e. Coli malate dehydrogenase
Source: Escherichia coli. Organism_taxid: 562. Gene: mdh. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (312 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1ie3
Crystal structure of r153c e. Coli malate dehydrogenase
Source: Escherichia coli. Organism_taxid: 562. Gene: mdh. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (312 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group PYR is 66.00% similar to enzyme reactant (S)-malate
  Het Group NAD corresponds to enzyme reactant NAD(+)
1iz9
Crystal structure of malate dehydrogenase from thermus therm hb8
Source: Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (327 residues) CATH domains: 3.40.50.720 3.90.110.10
1mld
Refined structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases
Source: Sus scrofa. Pig. Organism_taxid: 9823
Chains: A, B, C, D (313 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group CIT is 69.00% similar to enzyme reactant (S)-malate
1o6z
1.95 a resolution structure of (r207s,r292s) mutant of malate dehydrogenase from the halophilic archaeon haloarcula marismortui (holo form)
Source: Haloarcula marismortui. Organism_taxid: 2238. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (303 residues) CATH domains: 3.90.110.10 3.40.50.720
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1ojs
2.9 a resolution structure of malate dehydrogenase from archaeoglobus fulgidus in complex with nadh.
Source: Archaeoglobus fulgidus. Organism_taxid: 224325. Strain: vc-16, dsmz 4304. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (294 residues) CATH domains: 3.40.50.720 3.90.110.10
1oju
2.8 a resolution structure of malate dehydrogenase from archaeoglobus fulgidus in complex with etheno-NAD.
Source: Archaeoglobus fulgidus. Organism_taxid: 224325. Strain: vc-16, dsmz 4304. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (294 residues) CATH domains: 3.40.50.720 3.90.110.10
1sev
Mature and translocatable forms of glyoxysomal malate dehydrogenase have different activities and stabilities but similar crystal structures
Source: Citrullus lanatus. Organism_taxid: 3654. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (313 residues) CATH domains: 3.40.50.720 3.90.110.10
1smk
Mature and translocatable forms of glyoxysomal malate dehydrogenase have different activities and stabilities but similar crystal structures
Source: Citrullus lanatus. Organism_taxid: 3654. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H (313 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group CIT is 69.00% similar to enzyme reactant (S)-malate
1ur5
Stabilization of a tetrameric malate dehydrogenase by introduction of a disulfide bridge at the dimer/dimer interface
Source: Chloroflexus aurantiacus. Organism_taxid: 1108. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, C (299 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1uxg
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface.
Source: Chloroflexus aurantiacus. Organism_taxid: 1108. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (308 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group FUM is 88.89% similar to enzyme reactant (S)-malate
  Het Group NAD corresponds to enzyme reactant NAD(+)
1uxh
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface
Source: Chloroflexus aurantiacus. Organism_taxid: 1108. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (308 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group FUM is 88.89% similar to enzyme reactant (S)-malate
  Het Group NAD corresponds to enzyme reactant NAD(+)
1uxi
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface
Source: Chloroflexus aurantiacus. Organism_taxid: 1108. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (308 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group FUM is 88.89% similar to enzyme reactant (S)-malate
  Het Group NAD corresponds to enzyme reactant NAD(+)
1uxj
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface
Source: Chloroflexus aurantiacus. Organism_taxid: 1108. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, C (299 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1uxk
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface
Source: Chloroflexus aurantiacus. Organism_taxid: 1108. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, C (296 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
1v9n
Structure of malate dehydrogenase from pyrococcus horikoshii
Source: Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chain: A (348 residues) CATH domains: 1.10.1530.10 3.30.1370.60
Bound ligands:   Het Group GOL is 50.00% similar to enzyme reactant (S)-malate
  Het Group NDP is 91.67% similar to enzyme reactant NAD(+)
1wze
Structural basis for alteration of cofactor specificity of malate dehydrogenase from thermus flavus
Source: Thermus thermophilus. Organism_taxid: 274. Strain: at-62. Gene: mdh. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (327 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD is 59.00% similar to enzyme reactant NAD(+)
1wzi
Structural basis for alteration of cofactor specificity of malate dehydrogenase from thermus flavus
Source: Thermus thermophilus. Organism_taxid: 274. Strain: at-62. Gene: mdh. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (327 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NDP is 72.00% similar to enzyme reactant NAD(+)
1y7t
Crystal structure of NAD(h)-depenent malate dehydrogenase complexed with NADPH
Source: Thermus thermophilus. Organism_taxid: 274. Strain: at-62. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (327 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group TRS is 41.00% similar to enzyme reactant (S)-malate
  Het Group NDP is 91.00% similar to enzyme reactant NAD(+)
2cmd
The crystal structure of e.Coli malate dehydrogenase: a complex of the apoenzyme and citrate at 1.87 angstroms resolution
Source: Escherichia coli. Organism_taxid: 562
Chain: A (312 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group CIT is 69.00% similar to enzyme reactant (S)-malate
2cvq
Crystal structure of NAD(h)-dependent malate dehydrogenasE C with NADPH
Source: Thermus thermophilus. Organism_taxid: 274. Strain: at-62. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (327 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group TRS is 41.67% similar to enzyme reactant (S)-malate
  Het Group NDP is 72.92% similar to enzyme reactant NAD(+)
2d4a
Structure of the malate dehydrogenase from aeropyrum pernix
Source: Aeropyrum pernix. Organism_taxid: 56636. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: B, A, D, C (301 residues) CATH domains: 3.40.50.720 3.90.110.10
2dfd
Crystal structure of human malate dehydrogenase type 2
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mdh2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (314 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group MLT corresponds to enzyme reactant (S)-malate
  Het Group NAD corresponds to enzyme reactant NAD(+)
2hlp
Crystal structure of the e267r mutant of a halophilic malate dehydrogenase in the apo form
Source: Haloarcula marismortui. Organism_taxid: 2238. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (303 residues) CATH domains: 3.90.110.10 3.40.50.720
2j5k
2.0 a resolution structure of the wild type malate dehydrogenase from haloarcula marismortui (radiation damage series)
Source: Haloarcula marismortui. Organism_taxid: 2238. Strain: hms174. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (303 residues) CATH domains: 3.40.50.720 3.90.110.10
2j5q
2.15 a resolution structure of the wild type malate dehydrogenase from haloarcula marismortui after first radiation burn (radiation damage series)
Source: Haloarcula marismortui. Organism_taxid: 2238. Strain: hms174. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (303 residues) CATH domains: 3.40.50.720 3.90.110.10
2j5r
2.25 a resolution structure of the wild type malate dehydrogenase from haloarcula marismortui after second radiation burn (radiation damage series)
Source: Haloarcula marismortui. Organism_taxid: 2238. Strain: hms174. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (303 residues) CATH domains: 3.40.50.720 3.90.110.10
2pwz
Crystal structure of the apo form of e.Coli malate dehydroge
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12
Chains: A, C, E, G (312 residues) CATH domains: 3.40.50.720 3.90.110.10
2x0i
2.9 a resolution structure of malate dehydrogenase from archaeoglobus fulgidus in complex with nadh
Source: Archaeoglobus fulgidus dsm 4304. Organism_taxid: 224325. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (294 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAI corresponds to enzyme reactant NAD(+)
2x0j
2.8 a resolution structure of malate dehydrogenase from archaeoglobus fulgidus in complex with etheno-NAD
Source: Archaeoglobus fulgidus dsm 4304. Organism_taxid: 224325. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (294 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group ENA is 95.65% similar to enzyme reactant NAD(+)
2x0r
R207s,r292s mutant of malate dehydrogenase from the halophilic archaeon haloarcula marismortui (holo form)
Source: Haloarcula marismortui. Organism_taxid: 2238. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (303 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
3d5t
Crystal structure of malate dehydrogenase from burkholderia pseudomallei
Source: Burkholderia pseudomallei. Organism_taxid: 320372. Strain: 1710b. Gene: mdh, burps1710b_a0795. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (321 residues) CATH domains: 3.40.50.720 3.90.110.10
3gvh
Crystal structure of lactate/malate dehydrogenase from brucella melitensis
Source: Brucella melitensis biovar abortus 2308. Organism_taxid: 359391. Gene: mdh, bab1_1927. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (318 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
3gvi
Crystal structure of lactate/malate dehydrogenase from brucella melitensis in complex with adp
Source: Brucella melitensis biovar abortus 2308. Organism_taxid: 359391. Gene: mdh, bab1_1927. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (314 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group ADP is 61.00% similar to enzyme reactant NAD(+)
3hhp
Malate dehydrogenase open conformation
Source: Escherichia coli k-12. Organism_taxid: 83333. Gene: mdh, b3236, jw3205. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (312 residues) CATH domains: 3.40.50.720 3.90.110.10
3nep
1.55a resolution structure of malate dehydrogenase from sali ruber
Source: Salinibacter ruber. Organism_taxid: 309807. Strain: dsm 13855
Chain: X (305 residues) CATH domains: 3.40.50.720 3.90.110.10
3p7m
Structure of putative lactate dehydrogenase from francisella tularensis subsp. Tularensis schu s4
Source: Francisella tularensis. Organism_taxid: 119856. Strain: tularensis. Gene: ftt_0535c, mdh. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (318 residues) CATH domains: 3.40.50.720 3.90.110.10
3tl2
Crystal structure of bacillus anthracis str. Ames malate deh in closed conformation.
Source: Bacillus anthracis. Anthrax,anthrax bacterium. Organism_taxid: 1392. Strain: ames. Gene: bas4486, ba_4837, gbaa_4837, mdh. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (312 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group EDO is 44.44% similar to enzyme reactant (S)-malate
4bgt
1.70 a resolution structure of the malate dehydrogenase from chloroflexus aurantiacus
Source: Chloroflexus aurantiacus. Organism_taxid: 1108
Chains: A, D (309 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group ACT is 44.44% similar to enzyme reactant (S)-malate
4bgu
1.50 a resolution structure of the malate dehydrogenase from haloferax volcanii
Source: Synthetic: yes. Haloferax volcanii. Organism_taxid: 2246. Other_details: complete gene was synthesized by genecust eu company
Chains: A, B, C, D (303 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group TRS is 41.67% similar to enzyme reactant (S)-malate
4bgv
1.8 a resolution structure of the malate dehydrogenase from picrophilus torridus in its apo form
Source: Picrophilus torridus. Organism_taxid: 82076. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: complete gene was synthesized by genecust eu company
Chains: A, B, C, D (323 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group CIT is 69.23% similar to enzyme reactant (S)-malate
4cl3
1.70 a resolution structure of the malate dehydrogenase from chloroflexus aurantiacus
Source: Chloroflexus sp. Y-400-fl. Organism_taxid: 480224. Atcc: 2936. Other_details: dsm 63
Chains: A, D (309 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group ACT is 44.44% similar to enzyme reactant (S)-malate
4e0b
2.17 angstrom resolution crystal structure of malate dehydro from vibrio vulnificus cmcp6
Source: Vibrio vulnificus. Organism_taxid: 216895. Strain: cmcp6. Gene: mdh, vv1_0673. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (305 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group ACT is 44.44% similar to enzyme reactant (S)-malate
4h7p
Crystal structure of a putative cytosolic malate dehydrogena leishmania major friedlin
Source: Leishmania major. Organism_taxid: 347515. Strain: friedlin. Gene: cmdh, lmjf_28_2860. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (313 residues) CATH domains: 3.40.50.720 3.90.110.10
4i1i
Crystal structure of a putative cytosolic malate dehydrogena leishmania major friedlin in complex with NAD
Source: Leishmania major. Organism_taxid: 347515. Strain: friedlin. Gene: cmdh, lmjf_28_2860. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (320 residues) CATH domains: 3.40.50.720 3.90.110.10
4jco
1.7 a resolution structure of wild type malate dehydrogenase haloarcula marismortui
Source: Haloarcula marismortui. Organism_taxid: 2238. Strain: hms174. Gene: mdh, rrnac2706. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (303 residues) CATH domains: 3.40.50.720 3.90.110.10
4kde
Crystal structure of the apo form of thermus thermophilus ma dehydrogenase
Source: Thermus thermophilus. Organism_taxid: 274. Gene: mdh. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (331 residues) CATH domains: 3.40.50.720 3.90.110.10
4kdf
Crystal structure of thermus thermophilus malate dehydrogena complex with NAD
Source: Thermus thermophilus. Organism_taxid: 274. Gene: mdh. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (317 residues) CATH domains: 3.40.50.720 3.90.110.10
4mdh
Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-angstroms resolution
Source: Sus scrofa. Pig. Organism_taxid: 9823
Chains: A, B (334 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligand:   Het Group NAD corresponds to enzyme reactant NAD(+)
4ror
Crystal structure of malate dehydrogenase from methylobacter extorquens
Source: Methylobacterium extorquens. Organism_taxid: 419610. Strain: pa1. Gene: mdh, mext_1643. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (319 residues) CATH domains: 3.40.50.720 3.90.110.10
4ros
Crystal structure of methylobacterium extorquens malate dehy complexed with oxaloacetate and adenosine-5-diphosphoribose
Source: Methylobacterium extorquens. Organism_taxid: 419610. Strain: pa1. Gene: mdh, mext_1643. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (318 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group OAA corresponds to enzyme reactant (S)-malate
  Het Group APR is 77.78% similar to enzyme reactant NAD(+)
4tvo
Structure of malate dehydrogenase from mycobacterium tubercu
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: atcc 25618 / h37rv. Gene: mdh, rvbd_1240. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (328 residues)
5mdh
Crystal structure of ternary complex of porcine cytoplasmic dehydrogenase alpha-ketomalonate and tnad at 2.4 angstroms
Source: Sus scrofa. Pig. Organism_taxid: 9823. Organ: heart. Tissue: muscle. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (333 residues) CATH domains: 3.40.50.720 3.90.110.10
Bound ligands:   Het Group MAK is 54.55% similar to enzyme reactant (S)-malate
  Het Group NAD corresponds to enzyme reactant NAD(+)