Structure of PDB 3zh2 Chain D Binding Site BS01
Receptor Information
>3zh2 Chain D (length=311) Species:
36329
(Plasmodium falciparum 3D7) [
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PKAKIVLVGSGMIGGVMATLIVQKNLGDVVLFDIVKNMPHGKALDTSHTN
VMAYSNCKVSGSNTYDDLAGADVVIVTAGFTKAPDKEWNRDDLLPLNNKI
MIEIGGHIKKNCPNAFIIVVTNPVDVMVQLLHQHSGVPKNKIIGLGGVLD
TSRLKYYISQKLNVCPRDVNAHIVGAHGNKMVLLKRYITVGGIPLQEFIN
NKLISDAELEAIFDRTVNTALEIVNLHASPYVAPAAAIIEMAESYLKDLK
KVLICSTLLEGQYGHSDIFGGTPVVLGANGVEQVIELQLNSEEKAKFDEA
IAETKRMKALA
Ligand information
>3zh2 Chain G (length=27) [
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ctgggcggtagaaccatagtgacccag
Receptor-Ligand Complex Structure
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PDB
3zh2
Structural Basis for Discriminatory Recognition of Plasmodium Lactate Dehydrogenase by a DNA Aptamer
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
G13 I36 V37 M40 K44 A80 F82 K84 I105
Binding residue
(residue number reindexed from 1)
G11 I34 V35 M38 K42 A78 F80 K82 I100
Binding affinity
PDBbind-CN
: Kd=42nM
Enzymatic activity
Catalytic site (original residue number in PDB)
R95 D155 R158 H182
Catalytic site (residue number reindexed from 1)
R90 D150 R153 H177
Enzyme Commision number
1.1.1.27
: L-lactate dehydrogenase.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0004459
L-lactate dehydrogenase activity
GO:0005515
protein binding
GO:0016491
oxidoreductase activity
GO:0016616
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0030060
L-malate dehydrogenase (NAD+) activity
Biological Process
GO:0006096
glycolytic process
GO:0019752
carboxylic acid metabolic process
Cellular Component
GO:0005737
cytoplasm
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External links
PDB
RCSB:3zh2
,
PDBe:3zh2
,
PDBj:3zh2
PDBsum
3zh2
PubMed
24043813
UniProt
Q76NM3
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