9DHK: RMI1-RMI2

RMI1-RMI2 bound to cyclic peptide L3. Determined by X-ray diffraction at 2.35 Å resolution. Released 2 Jul 2025.

Method: X-ray diffraction
Resolution: 2.35 Å
Organisms: Homo sapiens, synthetic construct
Chains: 12
Atoms: 9,476
Mol. weight: 135.96 kDa
Released: 2 Jul 2025

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

Secondary structure: helices and β-sheets

9DHK contains 40 α-helices and 79 β-strands across 12 chains. 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: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	492	1	1
α-helix	494-499	6
β-strand	506-517	12	1
β-strand	522	1	2
α-helix	524-526	3
β-strand	529	1	2
β-strand	531-535	5	1
β-strand	540-545	6	1
α-helix	547-554	8
α-helix	558-564	7
α-helix	568-587	20
β-strand	589-597	9	1
β-strand	602-609	8	1
α-helix	613-622	10

Chain B: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	16	1	3
β-strand	23-24	2	4
α-helix	27-33	7
β-strand	34-37	4	5
β-strand	40-45	6	5
β-strand	50-55	6	5
β-strand	57-68	12	4
β-strand	71-76	6	4
β-strand	79-84	6	4
α-helix	86-88	3
β-strand	101-110	10	4
β-strand	116-124	9	4
α-helix	130-144	15

Chains C, F, I and L: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	103-105	3	3
β-strand	109-111	3	3

Chain D: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	483-485	3
β-strand	492	1	6
α-helix	494-499	6
β-strand	506-517	12	6
β-strand	522	1	7
α-helix	524-526	3
β-strand	529	1	7
β-strand	531-535	5	6
β-strand	540-545	6	6
α-helix	547-554	8
α-helix	558-564	7
α-helix	568-587	20
β-strand	589-597	9	6
α-helix	598-600	3
β-strand	602-609	8	6
α-helix	613-622	10

Chain E: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	16	1	6
β-strand	23-24	2	8
α-helix	27-33	7
β-strand	34-37	4	9
β-strand	40-45	6	9
β-strand	50-54	5	9
β-strand	58-68	11	8
β-strand	71-76	6	8
β-strand	79-84	6	8
α-helix	86-88	3
β-strand	101-110	10	8
β-strand	116-124	9	8
α-helix	130-145	16

Chain G: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	483-485	3
β-strand	492	1	10
α-helix	494-499	6
β-strand	506-517	12	10
β-strand	522	1	11
α-helix	524-526	3
β-strand	529	1	11
β-strand	531-535	5	10
β-strand	540-545	6	10
α-helix	547-554	8
α-helix	558-564	7
α-helix	568-587	20
β-strand	589-597	9	10
α-helix	598-600	3
β-strand	602-609	8	10
α-helix	613-623	11

Chain H: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	16	1	12
β-strand	23-24	2	13
α-helix	27-33	7
β-strand	34-35	2	14
β-strand	42-45	4	14
β-strand	50-54	5	14
β-strand	58-68	11	13
β-strand	71-76	6	13
β-strand	79-84	6	13
α-helix	86-88	3
β-strand	101-110	10	13
β-strand	116-124	9	13
α-helix	130-144	15

Chain J: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	494-499	6
β-strand	506-517	12	15
β-strand	522	1	16
α-helix	524-526	3
β-strand	529	1	16
β-strand	531-535	5	15
β-strand	540-545	6	15
α-helix	547-554	8
α-helix	558-564	7
α-helix	568-587	20
β-strand	589-597	9	15
β-strand	602-609	8	15
α-helix	613-622	10

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RecQ-mediated genome instability protein 1	A, D, J	protein	152	Homo sapiens	Q9H9A7 (AlphaFold model)
RecQ-mediated genome instability protein 2	B, K	protein	147	Homo sapiens	Q96E14 (AlphaFold model)
RecQ-mediated genome instability protein 2	E	protein	135	Homo sapiens	Q96E14 (AlphaFold model)
RecQ-mediated genome instability protein 1	G	protein	145	Homo sapiens	Q9H9A7 (AlphaFold model)
RecQ-mediated genome instability protein 2	H	protein	139	Homo sapiens	Q96E14 (AlphaFold model)
L3 peptide	C, F, I, L	protein	15	synthetic construct

Sequence of entity 1 (A, D, J), FASTA

>9DHK_1 RecQ-mediated genome instability protein 1 (chains A, D, J)
MENSINLSIAMDLYSPPFVYLSVLMASKPKEVTTVKVKAFIVTLTGNLSSSGGIWSITAK
VSDGTAYLDVDFVDEILTSLIGFSVPEMKQSKKDPLQYQKFLEGLQKCQRDLIDLCCLMT
ISFNPSLSKAMVLALQDVNMEHLENLKKRLNK

Sequence of entity 2 (B, K), FASTA

>9DHK_2 RecQ-mediated genome instability protein 2 (chains B, K)
MAAAADSFSGGPAGVRLPRSPPLKVLAEQLRRDAEGGPGAWRLSRAAAGRGPLDLAAVWM
QGRVVMADRGEARLRDPSGDFSVRGLERVPRGRPCLVPGKYVMVMGVVQACSPEPCLQAV
KMTDLSDNPIHESMWELEVEDLHRNIP

Sequence of entity 3 (E), FASTA

>9DHK_3 RecQ-mediated genome instability protein 2 (chains E)
XGVRLPRSPPLKVLAEQLRRDAEGGPGAWRLSRAAAGRGPLDLAAVWMQGRVVMADRGEA
RLRDPSGDFSVRGLERVPRGRPCLVPGKYVMVMGVVQACSPEPCLQAVKMTDLSDNPIHE
SMWELEVEDLHRNIP

Sequence of entity 4 (G), FASTA

>9DHK_4 RecQ-mediated genome instability protein 1 (chains G)
XIAMDLYSPPFVYLSVLMASKPKEVTTVKVKAFIVTLTGNLSSSGGIWSITAKVSDGTAY
LDVDFVDEILTSLIGFSVPEMKQSKKDPLQYQKFLEGLQKCQRDLIDLCCLMTISFNPSL
SKAMVLALQDVNMEHLENLKKRLNK

Sequence of entity 5 (H), FASTA

>9DHK_5 RecQ-mediated genome instability protein 2 (chains H)
XXXXXXVRLPRSPPLKVLAEQLRRDAEGGPGAWRLSRAAAGRGPLDLAAVWMQGRVVMAD
RGEARLRDPSGDFSVRGLERVPRGRPCLVPGKYVMVMGVVQACSPEPCLQAVKMTDLSDN
PIHESMWELEVEDLHRNIP

Sequence of entity 6 (C, F, I, L), FASTA

>9DHK_6 L3 peptide (chains C, F, I, L)
XYRLWFFQTYKLPCX

Primary citation

Potent Cyclic Peptide Inhibitors Disrupt the FANCM-RMI Interaction. Alcock, L.J., Gao, T., Bythell-Douglas, R. et al. J Med Chem (2025) 68:12615-12625. DOI 10.1021/acs.jmedchem.5c00365 · PubMed

Other PDB entries of the same protein (UniProt Q9H9A7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3MXN 1.55 Å, Crystal structure of the RMI core complex
7XUV 1.6 Å, Crystal structure of RPA70N-RMI1 fusion
3NBH 2.0 Å, Crystal structure of human RMI1C-RMI2 complex
3NBI 2.0 Å, Crystal structure of human RMI1 N-terminus
9PFD 2.01 Å, RMI1-RMI2 bound to synthetic peptide P4Ser
9DI4 2.7 Å, RMI1-RMI2 bound to cyclic peptide L4
4CGY 2.85 Å, Crystal structure of the human topoisomerase III alpha-RMI1 complex
4CHT 3.25 Å, Crystal structure of the human topoisomerase III alpha-RMI1 complex with bound calcium ion
4DAY 3.3 Å, Crystal structure of the RMI core complex with MM2 peptide from FANCM

Browse structure collections

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