Structure of PDB 6qas Chain A

Receptor sequence
>6qasA (length=274) Species: 9606 (Homo sapiens) [Search protein sequence]
TETVGKFEFSRKDLIGHGAFAVVFKGRHRAAHDLEVAVKCINKKNLAKSQ
TLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHAM
RTLSEDTIRLFLQQIAGAMRLLHSKGIIHRDLKPQNILLSNPAGRRANPN
SIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSI
GTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPTIPRETSAPLRQLLLA
LLQRNHKDRMDFDEFFHHPFLDAS
3D structure
PDB6qas Conservation of structure, function and inhibitor binding in UNC-51-like kinase 1 and 2 (ULK1/2).
ChainA
Resolution1.75 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) D138 K140 Q142 N143 D165 S184
Catalytic site (residue number reindexed from 1) D131 K133 Q135 N136 D158 S177
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 34W A I22 G23 V30 A44 M92 Y94 C95 G98 L145 I15 G16 V23 A37 M85 Y87 C88 G91 L138
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0010506 regulation of autophagy

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6qas, PDBe:6qas, PDBj:6qas
PDBsum6qas
PubMed30782972
UniProtO75385|ULK1_HUMAN Serine/threonine-protein kinase ULK1 (Gene Name=ULK1)

[Back to BioLiP]