Structure of PDB 6nfy Chain B

Receptor sequence
>6nfyB (length=285) Species: 9606 (Homo sapiens) [Search protein sequence]
GSNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVS
TLQKEILILKTCRHANIVAYHGSYLWLQKLWICMEFCGAGSLQDIYQVTG
SLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFG
ISAQIGATLARRLSFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIE
LAELQPPLFDVHPLRVLFLMTKSGYQPPRLKEKGKWSAAFHNFIKVTLTK
SPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLK
3D structure
PDB6nfy Multiple conformational states of the HPK1 kinase domain in complex with sunitinib reveal the structural changes accompanying HPK1 trans-regulation.
ChainB
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) D130 K132 A134 N135 D148 A157 T168
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 B L23 A44 M91 E92 F93 C94 G95 A96 G97 D101 L144 A154 L16 A37 M84 E85 F86 C87 G88 A89 G90 D94 L137 A147 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

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Molecular Function
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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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