Structure of PDB 2pml Chain X Binding Site BS01

Receptor Information

>2pml Chain X (length=340) Species: 5833 (Plasmodium falciparum)

GPLGSMKDILSNYSNLIYLNKYVKEKDKYINDYRIIRTLNQGKFNKIILC
EKDNKFYALKKYEKSLLEKKRDFTKSNNDKISIKSKYDDFKNELQIITDI
KNEYCLTCEGIITNYDEVYIIYEYMENDSILKFDEYFFVLDKNYTCFIPI
QVIKCIIKSVLNSFSYIHNEKNICHRDVKPSNILMDKNGRVKLSDFGESE
YMVDKKIKGSRGTYEFMPPEFFSNESSYNGAKVDIWSLGICLYVMFYNVV
PFSLKISLVELFNNIRTKNIEYPLDRNHFLYPLTNFLSNEDIDFLKLFLR
KNPAERITSEDALKHEWLADTNIEDLREFSKELYKKRKKL

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 2pml Chain X Residue 383

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2pml Structures of PfPK7 an atypical protein kinase from P. falciparum identify a novel activation motif and leads for inhibitor design
• Resolution: 2.6 Å
• Binding residue (original residue number in PDB): N177 D190
• Binding residue (residue number reindexed from 1): N182 D195
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): N177 D190
• Catalytic site (residue number reindexed from 1): N182 D195
• Enzyme Commision number: 2.7.12.2: mitogen-activated protein kinase kinase.

Gene Ontology

Molecular Function

• GO:0004672 protein kinase activity
• GO:0004708 MAP kinase kinase activity
• GO:0005524 ATP binding
• GO:0016740 transferase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0000165 MAPK cascade
• GO:0006468 protein phosphorylation

External links

• PDB: RCSB:2pml, PDBe:2pml, PDBj:2pml
• PDBsum: 2pml
• UniProt: O96214