Structure of PDB 3zh2 Chain A Binding Site BS01

Receptor Information

>3zh2 Chain A (length=314) Species: 36329 (Plasmodium falciparum 3D7)

PKAKIVLVGSGMIGGVMATLIVQKNLGDVVLFDIVKNMPHGKALDTSHTN
VMAYSNCKVSGSNTYDDLAGADVVIVTAGFTKAPGKSDKEWNRDDLLPLN
NKIMIEIGGHIKKNCPNAFIIVVTNPVDVMVQLLHQHSGVPKNKIIGLGG
VLDTSRLKYYISQKLNVCPRDVNAHIVGAHGNKMVLLKRYITVGGIPLQE
FINNKLISDAELEAIFDRTVNTALEIVNLHASPYVAPAAAIIEMAESYLK
DLKKVLICSTLLEGQYGHSDIFGGTPVVLGANGVEQVIELQLNSEEKAKF
DEAIAETKRMKALA

Ligand information

>3zh2 Chain E (length=27)

ctgggcggtagaaccatagtgacccag

Receptor-Ligand Complex Structure

Structure summary

• 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): D35 I36 A80 F82 K84 A85 P86 G87 K88 S89 D90 V229 H232 A233 S234
• Binding residue (residue number reindexed from 1): D33 I34 A78 F80 K82 A83 P84 G85 K86 S87 D88 V227 H230 A231 S232
• 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): R93 D153 R156 H180
• 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

External links

• PDB: RCSB:3zh2, PDBe:3zh2, PDBj:3zh2
• PDBsum: 3zh2
• PubMed: 24043813
• UniProt: Q76NM3