Structure of PDB 2pmo Chain X

Receptor sequence
>2pmoX (length=340) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
GPLGSMKDILSNYSNLIYLNKYVKEKDKYINDYRIIRTLNQGKFNKIILC
EKDNKFYALKKYEKSLLEKKRDFTKSNNDKISIKSKYDDFKNELQIITDI
KNEYCLTCEGIITNYDEVYIIYEYMENDSILKFDEYFFVLDKNYTCFIPI
QVIKCIIKSVLNSFSYIHNEKNICHRDVKPSNILMDKNGRVKLSDFGESE
YMVDKKIKGSRGTYEFMPPEFFSNESSYNGAKVDIWSLGICLYVMFYNVV
PFSLKISLVELFNNIRTKNIEYPLDRNHFLYPLTNFLSNEDIDFLKLFLR
KNPAERITSEDALKHEWLADTNIEDLREFSKELYKKRKKL
3D structure
PDB2pmo Structures of P. falciparum protein kinase 7 identify an activation motif and leads for inhibitor design.
ChainX
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) 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 HMD X I42 A53 K55 L101 Y117 E118 Y119 M120 D123 L179 D190 I47 A58 K60 L106 Y122 E123 Y124 M125 D128 L184 D195
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004708 MAP kinase kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0044024 histone H2AS1 kinase activity
Biological Process
GO:0000165 MAPK cascade
GO:0006338 chromatin remodeling
GO:0006468 protein phosphorylation
GO:0016310 phosphorylation
GO:0044773 mitotic DNA damage checkpoint signaling
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2pmo, PDBe:2pmo, PDBj:2pmo
PDBsum2pmo
PubMed18275814
UniProtQ7YTF7

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