Structure of PDB 5lw1 Chain E

Receptor sequence
>5lw1E (length=355) Species: 9606 (Homo sapiens) [Search protein sequence]
NNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKL
SRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIV
MELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNI
VVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVD
LWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVR
TYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDAS
KRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIY
KEVMD
3D structure
PDB5lw1 Structural Basis for the Selective Inhibition of c-Jun N-Terminal Kinase 1 Determined by Rigid DARPin-DARPin Fusions.
ChainE
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D151 K153 N156 D169 T188
Catalytic site (residue number reindexed from 1) D144 K146 N149 D162 T181
Enzyme Commision number 2.7.11.24: mitogen-activated protein 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 E M121 R127 Y130 S161 V323 W324 E329 M114 R120 Y123 S154 V316 W317 E322
BS02 ADN E V40 M108 M111 N114 S155 L168 V33 M101 M104 N107 S148 L161
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004707 MAP 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:5lw1, PDBe:5lw1, PDBj:5lw1
PDBsum5lw1
PubMed29126898
UniProtP45983|MK08_HUMAN Mitogen-activated protein kinase 8 (Gene Name=MAPK8)

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