9OG8: WRN

Crystal structure of WRN in complex with compound 43. Determined by X-ray diffraction at 1.66 Å resolution. Released 18 Jun 2025.

Method: X-ray diffraction
Resolution: 1.66 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,686
Mol. weight: 49.06 kDa
Ligands: A1CA5, ZN
Released: 18 Jun 2025

Explore 9OG8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9OG8 contains 24 α-helices and 18 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: 24 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	524	1	1
α-helix	531-533	3
α-helix	534-544	11
β-strand	548	1	1
α-helix	551-563	13
β-strand	567-571	5	2
α-helix	578-588	11
β-strand	591-595	5	2
α-helix	599-611	13
β-strand	616-618	3	2
α-helix	625-632	8
β-strand	638-641	4	2
α-helix	643-648	6
α-helix	650-659	10
β-strand	662-667	6	2
α-helix	670-673	4
α-helix	682-689	8
α-helix	690-693	4
β-strand	699-703	5	2
α-helix	708-717	10
β-strand	724-728	5	2
β-strand	735-741	7	3
α-helix	746-750	5
α-helix	751-753	3
β-strand	754-756	3	4
β-strand	761-763	3	4
β-strand	767-770	4	3
α-helix	774-785	12
β-strand	791-794	4	3
α-helix	800-811	12
β-strand	817-820	4	3
α-helix	823-825	3
β-strand	835-839	5	3
α-helix	845-852	8
β-strand	862-868	7	3
α-helix	873-875	3
α-helix	877-880	4
α-helix	886-904	19
α-helix	909-917	9
α-helix	920-925	6
β-strand	936	1	3
α-helix	937-943	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN	A	protein	424	Homo sapiens	Q14191 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9OG8_1 Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN (chains A)
SGSDFLWPAPNEEQVTCLKMYFGHSSFKPVQWKVIHSVLEERRDNVAVMATGYGKSLCFQ
YPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVT
PEYCSGNMGLLQQLEADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVAL
TATASSSIREDIVRCLNLRNPQITCTGFDRPNLYLEVRRKTGNILQDLQPFLVKTSSHWE
FEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATI
AFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTE
IRNEKFRLYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQVQKASLGIMGTEKCCDNCRSR
LDHC

Ligands and cofactors

ID	Name	Formula	Copies
A1CA5	(3R,4S)-N-[(2R)-3-cyclohexyl-1-(methylamino)-1-oxopropan-2-yl]-4-{3-[6-(ethanes…	C37 H50 F N7 O7 S	1
ZN	Zinc ion	Zn	1

Primary citation

Validation, Key Pharmacophores, and X-ray Cocrystal Structures of Novel Biochemically and Cellularly Active WRN Inhibitors Derived from a DNA-Encoded Library Screen. Tong, Y., Baker, K.A., Chapman, A.M. et al. J Med Chem (2025) 68:12434-12456. DOI 10.1021/acs.jmedchem.4c03029 · PubMed

Other PDB entries of the same protein (UniProt Q14191 (AlphaFold model), which also has an AlphaFold model), best resolution first:

10AK 1.37 Å, Crystal Structure of Human WRN helicase with compound 4
7GQU 1.54 Å, Crystal Structure of Werner helicase fragment 517-945 in covalent complex with…
9OWB 1.56 Å, Human WRN helicase in complex with allosteric ligand Compound 6
7GQS 1.57 Å, Crystal Structure of Werner helicase fragment 517-945 in complex with ADP
9MJU 1.58 Å, Crystal structure of WRN helicase with allosteric fragment 1
7XUT 1.6 Å, Crystal structure of RPA70N-WRN fusion
8PFP 1.6 Å, Crystal structure of WRN helicase domain in complex with ATPgammaS
9MJY 1.63 Å, Crystal structure of WRN helicase with bound allosteric compound 1
9OWC 1.67 Å, Human WRN helicase in complex with allosteric ligand Compound 7
9MJZ 1.7 Å, Crystal structure of WRN helicase with bound allosteric compound 3
9MJT 1.73 Å, Crystal structure of apo WRN helicase in Form D
9MJX 1.73 Å, Crystal structure of WRN helicase with bound allosteric fragment 4

Browse structure collections

About this viewer

MolViewer shows 9OG8 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.