5CI7: ULK1

Structure of ULK1 bound to a selective inhibitor. Determined by X-ray diffraction at 1.74 Å resolution. Released 26 Aug 2015.

Method: X-ray diffraction
Resolution: 1.74 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,464
Mol. weight: 33.08 kDa
Ligands: 51W
Released: 26 Aug 2015

Explore 5CI7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5CI7 contains 12 α-helices and 14 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	9-11	3	1
β-strand	14-25	12	1
β-strand	28-35	8	1
β-strand	42-47	6	1
α-helix	50-52	3
α-helix	53-67	15
β-strand	75	1	2
β-strand	78-83	6	1
β-strand	88-93	6	1
β-strand	99	1	2
α-helix	100-106	7
α-helix	112-132	21
β-strand	134-135	2	3
α-helix	141-143	3
β-strand	144-147	4	2
α-helix	156-158	3
β-strand	160-163	4	2
β-strand	170-171	2	3
β-strand	178	1	4
α-helix	190-193	4
β-strand	198	1	4
α-helix	201-216	16
α-helix	226-235	10
α-helix	249-258	10
α-helix	269-273	5
α-helix	276-278	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase ULK1	A	protein	287	Homo sapiens	O75385 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5CI7_1 Serine/threonine-protein kinase ULK1 (chains A)
GGGSMEPGRGGTETVGKFEFSRKDLIGHGAFAVVFKGRHRAAHDLEVAVKCINKKNLAKS
QTLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHAMRTLSEDTIR
LFLQQIAGAMRLLHSKGIIHRDLKPQNILLSNPAGRRANPNSIRVKIADFGFARYLQSNM
MAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKN
KTLVPTIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASPS

Ligands and cofactors

ID	Name	Formula	Copies
51W	N-[3-({4-[(3-aminopropyl)amino]-5-iodopyrimidin-2-yl}amino)phenyl]pyrrolidine-1…	C18 H24 I N7 O	1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Discovery and structure of a new inhibitor scaffold of the autophagy initiating kinase ULK1. Lazarus, M.B., Shokat, K.M. Bioorg Med Chem (2015) 23:5483-5488. DOI 10.1016/j.bmc.2015.07.034 · PubMed

Other PDB entries of the same protein (UniProt O75385 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6HYO 1.07 Å, Structure of ULK1 LIR motif bound to GABARAP
4WNO 1.56 Å, Structure of ULK1 bound to an inhibitor
6MNH 1.73 Å, ULK1 Unc-51 like autophagy activating kinase in complex with inhibitor BTC
6QAS 1.75 Å, Crystal structure of ULK1 in complexed with PF-03814735
8P5I 1.83 Å, Kinase domain of mutant human ULK1 in complex with compound XMD-17-51
8P5L 1.84 Å, Kinase domain of mutant human ULK1 in complex with compound MRT67307
4WNP 1.88 Å, Structure of ULK1 bound to a potent inhibitor
8P5H 1.94 Å, Kinase domain of mutant human ULK1 in complex with compound CCT241533
9SE8 2.0 Å, Crystal structure of ULK1 in complex with inhibitor SBP-5147
8P5G 2.02 Å, Kinase domain of wild type human ULK1 in complex with compound CCT241533
9F32 2.1 Å, Crystal structure of ULK1 with a covalent compound GCL 99
8P5J 2.16 Å, Kinase domain of mutant human ULK1 in complex with compound WZ4003

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