Structure of PDB 6ng0 Chain A

Receptor sequence
>6ng0A (length=289) Species: 9606 (Homo sapiens) [Search protein sequence]
PDIFNRDPRDHYDLLQRLGGGEVFKARDKVSGDLVALKMVKMEPDDDVST
LQKEILILKTCRHANIVAYHGSYLWLQKLWICMEFCGAGSLQDIYQVTGS
LSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGI
SALARRLEFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQP
PLFDVHPLRVLFLMTKSGYQPPRLKEKGKWSAAFHNFIKVTLTKSPKKRP
SATKMLSHQLVSQPGLNRGLILDLLDKLKNPGKGPSIGD
3D structure
PDB6ng0 Multiple conformational states of the HPK1 kinase domain in complex with sunitinib reveal the structural changes accompanying HPK1 trans-regulation.
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D137 K139 A141 N142 D155 T175
Catalytic site (residue number reindexed from 1) D129 K131 A133 N134 D147 T162
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 M91 F93 C94 G95 G97 D101 L144 D155 L18 A36 M83 F85 C86 G87 G89 D93 L136 D147 MOAD: Ki=10nM
PDBbind-CN: -logKd/Ki=8.19,Ki=0.0064uM
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:6ng0, PDBe:6ng0, PDBj:6ng0
PDBsum6ng0
PubMed31018963
UniProtQ92918|M4K1_HUMAN Mitogen-activated protein kinase kinase kinase kinase 1 (Gene Name=MAP4K1)

[Back to BioLiP]