Structure of PDB 5hto Chain E

Receptor sequence
>5htoE (length=305) Species: 5855 (Plasmodium vivax) [Search protein sequence]
KPKIVLVGSGMIGGVMATLIVQKNLGDVVMFDVVKNMPQGKALDTSHSNV
MAYSNCKVTGSNSYDDLKGADVVIVTAGFTKAPRDDLLPLNNKIMIEIGG
HIKNLCPNAFIIVVTNPVDVMVQLLFEHSGVPKNKIIGLGGVLDTSRLKY
YISQKLNVCPRDVNALIVGAHGNKMVLLKRYITVGGIPLQEFINNKKITD
EEVEGIFDRTVNTALEIVNLLASPYVAPAAAIIEMAESYLKDIKKVLVCS
TLLEGQYGHSNIFGGTPLVIGGTGVEQVIELQLNAEEKTKFDEAVAETKR
MKALI
3D structure
PDB5hto Crystal structure of a DNA aptamer bound to PvLDH elucidates novel single-stranded DNA structural elements for folding and recognition
ChainE
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 dna E G13 M14 D35 V36 V37 K38 M40 A80 G81 F82 I105 G10 M11 D32 V33 V34 K35 M37 A77 G78 F79 I94
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
PDBsum5hto
PubMed27725738
UniProtQ4PRK9

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