Structure of PDB 5byz Chain A

Receptor sequence
>5byzA (length=348) Species: 9606 (Homo sapiens) [Search protein sequence]
TFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAK
RTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQI
IHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELK
IGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWS
VGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAY
IQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL
AKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGI
3D structure
PDB5byz Discovery of a novel allosteric inhibitor-binding site in ERK5: comparison with the canonical kinase hinge ATP-binding site.
ChainA
Resolution1.65 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) D135 K137 S139 N140 D153 T177
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 4WE A I61 G62 Y66 K84 I115 L137 M140 D143 H145 Q146 L189 I14 G15 Y19 K37 I68 L90 M93 D96 H98 Q99 L142 MOAD: ic50=0.042uM
PDBbind-CN: -logKd/Ki=7.38,IC50=0.042uM
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:5byz, PDBe:5byz, PDBj:5byz
PDBsum5byz
PubMed27139631
UniProtQ13164|MK07_HUMAN Mitogen-activated protein kinase 7 (Gene Name=MAPK7)

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