Structure of PDB 5hto Chain E Binding Site BS01
Receptor Information
>5hto Chain E (length=305) Species:
5855
(Plasmodium vivax) [
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KPKIVLVGSGMIGGVMATLIVQKNLGDVVMFDVVKNMPQGKALDTSHSNV
MAYSNCKVTGSNSYDDLKGADVVIVTAGFTKAPRDDLLPLNNKIMIEIGG
HIKNLCPNAFIIVVTNPVDVMVQLLFEHSGVPKNKIIGLGGVLDTSRLKY
YISQKLNVCPRDVNALIVGAHGNKMVLLKRYITVGGIPLQEFINNKKITD
EEVEGIFDRTVNTALEIVNLLASPYVAPAAAIIEMAESYLKDIKKVLVCS
TLLEGQYGHSNIFGGTPLVIGGTGVEQVIELQLNAEEKTKFDEAVAETKR
MKALI
Ligand information
>5hto Chain F (length=30) [
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cgattggattgtgccggaagtgctggctcg
Receptor-Ligand Complex Structure
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PDB
5hto
Crystal structure of a DNA aptamer bound to PvLDH elucidates novel single-stranded DNA structural elements for folding and recognition
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
G13 M14 D35 V36 V37 K38 M40 A80 G81 F82 I105
Binding residue
(residue number reindexed from 1)
G10 M11 D32 V33 V34 K35 M37 A77 G78 F79 I94
Enzymatic activity
Catalytic site (original residue number in PDB)
R95 D155 R158 H182
Catalytic site (residue number reindexed from 1)
R84 D144 R147 H171
Enzyme Commision number
1.1.1.27
: L-lactate dehydrogenase.
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0003824
catalytic activity
GO:0004459
L-lactate dehydrogenase activity
GO:0016491
oxidoreductase activity
GO:0016616
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Biological Process
GO:0006089
lactate metabolic process
GO:0006090
pyruvate metabolic process
GO:0019752
carboxylic acid metabolic process
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Molecular Function
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Biological Process
External links
PDB
RCSB:5hto
,
PDBe:5hto
,
PDBj:5hto
PDBsum
5hto
PubMed
27725738
UniProt
Q4PRK9
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