Structure of PDB 2pml Chain X

Receptor sequence
>2pmlX (length=340) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
GPLGSMKDILSNYSNLIYLNKYVKEKDKYINDYRIIRTLNQGKFNKIILC
EKDNKFYALKKYEKSLLEKKRDFTKSNNDKISIKSKYDDFKNELQIITDI
KNEYCLTCEGIITNYDEVYIIYEYMENDSILKFDEYFFVLDKNYTCFIPI
QVIKCIIKSVLNSFSYIHNEKNICHRDVKPSNILMDKNGRVKLSDFGESE
YMVDKKIKGSRGTYEFMPPEFFSNESSYNGAKVDIWSLGICLYVMFYNVV
PFSLKISLVELFNNIRTKNIEYPLDRNHFLYPLTNFLSNEDIDFLKLFLR
KNPAERITSEDALKHEWLADTNIEDLREFSKELYKKRKKL
3D structure
PDB2pml Structures of PfPK7 an atypical protein kinase from P. falciparum identify a novel activation motif and leads for inhibitor design
ChainX
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 MN X N177 D190 N182 D195
BS02 ANP X N35 N40 I42 A53 K55 Y119 M120 D123 S176 L179 D190 N40 N45 I47 A58 K60 Y124 M125 D128 S181 L184 D195
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2pml, PDBe:2pml, PDBj:2pml
PDBsum2pml
PubMed
UniProtO96214

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