Structure of PDB 5hru Chain B

Receptor sequence
>5hruB (length=306) Species: 5855 (Plasmodium vivax) [Search protein sequence]
PKPKIVLVGSGMIGGVMATLIVQKNLGDVVMFDVVKNMPQGKALDTSHSN
VMAYSNCKVTGSNSYDDLKGADVVIVTAGFTKANRDDLLPLNNKIMIEIG
GHIKNLCPNAFIIVVTNPVDVMVQLLFEHSGVPKNKIIGLGGVLDTSRLK
YYISQKLNVCPRDVNALIVGAHGNKMVLLKRYITVGGIPLQEFINNKKIT
DEEVEGIFDRTVNTALEIVNLLASPYVAPAAAIIEMAESYLKDIKKVLVC
STLLEGQYGHSNIFGGTPLVIGGTGVEQVIELQLNAEEKTKFDEAVAETK
RMKALI
3D structure
PDB5hru Crystal structure of a DNA aptamer bound to PvLDH elucidates novel single-stranded DNA structural elements for folding and recognition
ChainB
Resolution1.71 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) R85 D145 R148 H172
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 B G13 M14 D35 V36 V37 M40 A80 G81 F82 I105 G11 M12 D33 V34 V35 M38 A78 G79 F80 I95
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:5hru, PDBe:5hru, PDBj:5hru
PDBsum5hru
PubMed27725738
UniProtQ4PRK9

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