9MJT: Apo WRN helicase in Form D

Crystal structure of apo WRN helicase in Form D. Determined by X-ray diffraction at 1.73 Å resolution. Released 14 Jan 2026.

Method: X-ray diffraction
Resolution: 1.73 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,649
Mol. weight: 50.71 kDa
Ligands: ZN
Released: 14 Jan 2026

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

Secondary structure: helices and β-sheets

9MJT contains 25 α-helices and 16 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: 25 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	531-533	3
α-helix	534-544	11
α-helix	551-558	8
α-helix	559-563	5
β-strand	567-570	4	1
α-helix	575-588	14
β-strand	591-595	5	1
α-helix	599-611	13
β-strand	616-618	3	1
α-helix	624-632	9
β-strand	638-641	4	1
α-helix	643-647	5
α-helix	650-659	10
β-strand	662-667	6	1
α-helix	670-673	4
α-helix	682-689	8
α-helix	690-693	4
β-strand	699-703	5	1
α-helix	708-717	10
α-helix	723	1
β-strand	724-727	4	1
β-strand	735-741	7	2
α-helix	746-750	5
α-helix	751-753	3
β-strand	755-756	2	3
β-strand	761-762	2	3
β-strand	767-770	4	2
α-helix	774-785	12
β-strand	791-794	4	2
α-helix	800-811	12
β-strand	817-820	4	2
β-strand	835-839	5	2
α-helix	845-852	8
β-strand	862-868	7	2
α-helix	873-875	3
α-helix	878-881	4
α-helix	886-904	19
α-helix	909-917	9
α-helix	920-924	5
β-strand	936	1	2
α-helix	937-940	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN	A	protein	443	Homo sapiens	Q14191 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9MJT_1 Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN (chains A)
NLGLPTKEEEEDDENEANEGEEDDDKDFLWPAPNEEQVTCLKMYFGHSSFKPVQWKVIHS
VLEERRDNVAVMATGYGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFL
GSAQSENVLTDIKLGKYRIVYVTPEYCSGNMGLLQQLEADIGITLIAVDEAHCISEWGHD
FRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFDRPNLYLEV
RRKTGNILQDLQPFLVKTSSHWEFEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMS
FSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDG
LQSSCHVLWAPADINLNRHLLTEIRNEKFRLYKLKMMAKMEKYLHSSRCRRQIILSHFED
KQVQKASLGIMGTEKCCDNCRSR

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Water and common crystallization additives (CL, EDO) are not listed.

Primary citation

WRN structural flexibility showcased through fragment-based lead discovery of inhibitors. Palte, R.L., Mandal, M., Sikorska, J. et al. Nat Commun (2026) 17:79-79. DOI 10.1038/s41467-025-66768-8 · 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
9OG8 1.66 Å, Crystal structure of WRN in complex with compound 43
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
9MJX 1.73 Å, Crystal structure of WRN helicase with bound allosteric fragment 4

Browse structure collections

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