Structure of PDB 3alo Chain A

Receptor sequence
>3aloA (length=289) Species: 9606 (Homo sapiens) [Search protein sequence]
WDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQ
LLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFDKFYKYVYS
VLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIK
LCDFGISGQLVDSIAKTRDAGCRPYMAPERIDPYDVRSDVWSLGITLYEL
ATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTK
DESKRPKYKELLKHPFILMYEERAVEVACYVCKILDQMP
3D structure
PDB3alo Crystal structures of MKK4 kinase domain reveal that substrate peptide binds to an allosteric site and induces an auto-inhibition state
ChainA
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) D229 K231 S233 N234 D247 D256 C266
Catalytic site (residue number reindexed from 1) D135 K137 S139 N140 D153 D162 C172
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 peptide A D96 F97 T98 H121 M128 Y165 A167 L168 F169 D2 F3 T4 H27 M34 Y71 A73 L74 F75
BS02 MG A N234 D247 N140 D153
BS03 ANP A I108 G109 G111 V116 A129 K131 M178 M181 K187 D229 K231 S233 N234 L236 D247 I14 G15 G17 V22 A35 K37 M84 M87 K93 D135 K137 S139 N140 L142 D153
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3alo, PDBe:3alo, PDBj:3alo
PDBsum3alo
PubMed20732303
UniProtP45985|MP2K4_HUMAN Dual specificity mitogen-activated protein kinase kinase 4 (Gene Name=MAP2K4)

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