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Drug-Target Interaction

Drug

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PubChem ID:971
Structure:
Synonyms:
04621_FLUKA
144-62-7
194131_ALDRICH
1o4n
1t5a
216451-38-6
241172_ALDRICH
2847-15-6
2dua
2hwg
319201_ALDRICH
319201_FLUKA
34287_FLUKA
34287_RIEDEL
35294_FLUKA
35294_RIEDEL
35295_FLUKA
35295_RIEDEL
38250_FLUKA
38250_RIEDEL
38255_FLUKA
38255_RIEDEL
4-02-00-01819 (Beilstein Handbook Reference)
547-66-0
553-91-3
553-91-3 (DILITHIUM)
63504-28-9
658537_ALDRICH
68487_FLUKA
75688_FLUKA
75688_SIAL
97993-78-7
AC1L1AFW
AC1Q28J7
Acide oxalique
Acide oxalique [French]
Acido ossalico
Acido ossalico [Italian]
Acidum oxalicum
AG-D-87878
AI3-26463
AIDS-071020
AIDS071020
Aktisal
Aquisal
AR-1K9315
BBL003000
bmse000106
BRN 0385686
C00209
Caswell No. 625
CCRIS 1454
CHEBI:16995
CHEMBL146755
DB03902
EINECS 205-634-3
EPA Pesticide Chemical Code 009601
Ethandisaeure
ethane-1,2-dioic acid
Ethanedioic acid
Ethanedioic acid (9CI)
Ethanedionic acid
F1B1B2D7-C290-4CE6-8550-F25B202AFADE
H2ox
HOOCCOOH
HSDB 1100
Kyselina stavelova
Kyselina stavelova [Czech]
LMFA01170031
LS-851
MAGNESIUM PERMANGANATE
NCGC00249170-01
NCI-C55209
NCIOpen2_000770
NCIOpen2_001022
NCIOpen2_001042
NCIOpen2_001202
NCIOpen2_008831
NSC 62774
NSC115893
NSC115893 (DILITHIUM)
NSC62774
Oxaalzuur
Oxaalzuur [Dutch]
Oxagel
Oxalate
Oxalate Ion
Oxalate standard for IC
Oxalic acid
Oxalic acid (8CI)
Oxalic acid solution
Oxalic acid standard solution
Oxalsaeure
Oxalsaeure [German]
OXD
Oxiric acid
OXL
S04-0160
STK379550
Ultraplast Activate S 52
WLN: QVVQ

Target

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Uniprot ID:MAOM_HUMAN
Synonyms:
Malic enzyme 2
NAD-dependent malic enzyme, mitochondrial
NAD-ME
EC-Numbers:1.1.1.38
Organism:Homo sapiens
Human
PDB IDs:1DO8 1EFK 1EFL 1GZ3 1GZ4 1PJ2 1PJ3 1PJ4 1PJL 1QR6
Structure:
1QR6

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----
----

References:

10700286
Structure of a closed form of human malic enzyme and implications for catalytic mechanism.. Z Yang; D L Floyd; G Loeber; L Tong (2000) Nature structural biology display abstract
Malic enzymes are widely distributed in nature and have many biological functions. The crystal structure of human mitochondrial NAD(P)+-dependent malic enzyme in a quaternary complex with NAD+, Mn++ and oxalate has been determined at 2.2 A resolution. The structures of the quaternary complex with NAD+, Mg++, tartronate or ketomalonate have been determined at 2.6 A resolution. The structures show the enzyme in a closed form in these complexes and reveal the binding modes of the cation and the inhibitors. The divalent cation is coordinated in an octahedral fashion by six ligating oxygens, two from the substrate/inhibitor, three from Glu 255, Asp 256 and Asp 279 of the enzyme, and one from a water molecule. The structural information has significant implications for the catalytic mechanism of malic enzymes and identifies Tyr 112 and Lys 183 as possible catalytic residues. Changes in tetramer organization of the enzyme are also observed in these complexes, which might be relevant for its cooperative behavior and allosteric control.
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