Structure of PDB 6nfy Chain A

Receptor sequence
>6nfyA (length=282) Species: 9606 (Homo sapiens) [Search protein sequence]
GSNRDPRDHYDLLQRLGGGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQ
KEILILKTCRHANIVAYHGSYLWLQKLWICMEFCGAGSLQDIYQVTGSLS
ELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGISA
QIGATLARRLSFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAE
LQPPLFDVHPLRVLFLMTKSGYQPPRLKEKGKWSAAFHNFIKVTLTKSPK
KRPSATKMLSHQLVSQPGLNRGLILDLLDKLK
3D structure
PDB6nfy Multiple conformational states of the HPK1 kinase domain in complex with sunitinib reveal the structural changes accompanying HPK1 trans-regulation.
ChainA
Resolution2.17 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D137 K139 A141 N142 D155 A164 T175
Catalytic site (residue number reindexed from 1) D127 K129 A131 N132 D145 A154 T165
Enzyme Commision number 2.7.11.1: non-specific serine/threonine 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 B49 A L23 A44 E92 F93 C94 G95 G97 D101 L144 L16 A34 E82 F83 C84 G85 G87 D91 L134 MOAD: Kd=16nM
PDBbind-CN: -logKd/Ki=7.80,Kd=16nM
BindingDB: Kd=16nM
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:6nfy, PDBe:6nfy, PDBj:6nfy
PDBsum6nfy
PubMed31018963
UniProtQ92918|M4K1_HUMAN Mitogen-activated protein kinase kinase kinase kinase 1 (Gene Name=MAP4K1)

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