Structure of PDB 5byy Chain A

Receptor sequence
>5byyA (length=338) Species: 9606 (Homo sapiens) [Search protein sequence]
FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKR
TLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQII
HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKI
GDFGMARGLYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEML
ARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQSLPPRQP
VPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDE
PDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREG
3D structure
PDB5byy Discovery of a novel allosteric inhibitor-binding site in ERK5: comparison with the canonical kinase hinge ATP-binding site.
ChainA
Resolution2.79 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D182 K184 S186 N187 D200 T224
Catalytic site (residue number reindexed from 1) D134 K136 S138 N139 D152 T168
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 4WG A I61 L137 M140 E141 L189 I13 L89 M92 E93 L141 PDBbind-CN: -logKd/Ki=7.01,IC50=0.098uM
BindingDB: Kd=80nM,IC50=300nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004707 MAP kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5byy, PDBe:5byy, PDBj:5byy
PDBsum5byy
PubMed27139631
UniProtQ13164|MK07_HUMAN Mitogen-activated protein kinase 7 (Gene Name=MAPK7)

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