1MIU: BRCA2-DSS1 complex

Structure of a BRCA2-DSS1 complex. Determined by X-ray diffraction at 3.1 Å resolution. Released 25 Sept 2002.

Method: X-ray diffraction
Resolution: 3.1 Å
Organisms: Homo sapiens, Mus musculus
Chains: 2
Atoms: 5,647
Mol. weight: 92.64 kDa
Ligands: HG
Released: 25 Sept 2002

Explore 1MIU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MIU contains 29 α-helices and 32 β-strands across 2 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: 27 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	2404-2420	17
α-helix	2430-2435	6
β-strand	2442-2443	2	1
α-helix	2446-2448	3
α-helix	2486-2489	4
β-strand	2500-2501	2	3
β-strand	2507-2508	2	3
α-helix	2509-2511	3
α-helix	2518-2527	10
α-helix	2538-2554	17
α-helix	2570-2580	11
α-helix	2581-2586	6
α-helix	2592-2597	6
β-strand	2604	1	4
β-strand	2607-2608	2	5
β-strand	2610-2611	2	6
β-strand	2642-2643	2	6
β-strand	2648-2649	2	6
α-helix	2655-2662	8
β-strand	2671	1	6
β-strand	2677	1	4
β-strand	2679-2680	2	7
β-strand	2696-2697	2	7
α-helix	2701-2703	3
β-strand	2707	1	2
β-strand	2714-2715	2	5
α-helix	2721-2722	2
α-helix	2726-2728	3
β-strand	2736-2746	11	8
α-helix	2747-2749	3
β-strand	2750	1	8
β-strand	2753-2754	2	9
β-strand	2760-2761	2	9
α-helix	2767-2778	12
α-helix	2782-2791	10
α-helix	2813-2817	5
α-helix	2822-2830	9
α-helix	2855-2871	17
α-helix	2873-2876	4
β-strand	2886	1	9
β-strand	2889-2896	8	8
β-strand	2904-2909	6	8
α-helix	2913-2918	6
β-strand	2924-2930	7	8
β-strand	2945-2957	13	8
α-helix	2961-2964	4
β-strand	2973	1	10
α-helix	2977-2980	4
β-strand	2990-3001	12	11
β-strand	3009-3013	5	11
β-strand	3019-3024	6	11
β-strand	3037-3044	8	11
β-strand	3056-3058	3	11
β-strand	3063-3065	3	11
α-helix	3074-3080	7
α-helix	3082-3085	4
α-helix	3090-3102	13

Chain B: 2 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	10-12	3
β-strand	13-14	2	1
β-strand	39	1	2
α-helix	59-62	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Deleted in split hand/split foot protein 1	B	protein	70	Homo sapiens	P60896 (AlphaFold model)
Breast Cancer type 2 susceptibility protein	A	protein	738	Mus musculus	P97929

Sequence of entity 1 (B), FASTA

>1MIU_1 Deleted in split hand/split foot protein 1 (chains B)
MSEKKQPVDLGLLEEDDEFEEFPAEDWAGLDEDEDAHVWEDNWDDDNVEDDFSNQLRAEL
EKHGYKMETS

Sequence of entity 2 (A), FASTA

>1MIU_2 Breast Cancer type 2 susceptibility protein (chains A)
NQKSTDGDREDGNDSHVRQFNKDLMSSLQSARDLQDMRIKNKERRHLRLQPGSLYLTKSS
TLPRISLQAAVGDRAPSACSPKQLYIYGVSKECINVNSKNAEYFQFDIQDHFGKEDLCAG
KGFQLADGGWLIPSNDGKAGKEEFYRALCDTPGVDPKLISSIWVANHYRWIVWKLAAMEF
AFPKEFANRCLNPERVLLQLKYRYDVEIDNSRRSALKKILERDDTAAKTLVLCISDIISP
STKVSETSGGKTSGEDANKVDTIELTDGWYAVRAQLDPPLMALVKSGKLTVGQKIITQGA
ELVGSPDACAPLEAPDSLRLKISANSTRPARWHSRLGFFRDPRPFPLPLSSLFSDGGNVG
CVDIIVQRVYPLQWVEKTVSGLYIFRSEREEEKEALRFAEAQQKKLEALFTKVHTEFKDH
EEDTTQRCVLSRTLTRQQVHALQDGAELYAAVQYASDPDHLEACFSEEQLRALNNYRQML
NDKKQARIQSEFRKALESAEKEEGLSRDVTTVWKLRVTSYKKKEKSALLSIWRPSSDLSS
LLTEGKRYRIYHLAVSKSKSKFERPSIQLTATKRTQYQQLPVSSETLLQVYQPRESLHFS
RLSDPAFQPPCSEVDVVGVVVSVVKPIGLAPLVYLSDECLNLLVVKFGIDLNEDIKPRVL
IAASNLQCQPESTSGVPTLFAGHFSIFSASPKEAYFQEKVNNLKHAIENIDTFYKEAEKK
LIHVLEGDSPKWSTPNKD

Ligands and cofactors

ID	Name	Formula	Copies
HG	Mercury (II) ion	Hg	5

Primary citation

BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure. Yang, H., Jeffrey, P.D., Miller, J. et al. Science (2002) 297:1837-1848. DOI 10.1126/science.297.5588.1837 · PubMed

Other PDB entries of the same protein (UniProt P60896 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3T5X 2.12 Å, PCID2:DSS1 Structure
9K53 2.5 Å, Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state ED2.1
9RV1 2.62 Å, Cryo-EM structure of the human UAP56-RNA - SAC3D1-PCID2-SEM1 complex
8USB 2.73 Å, Non-substrate-engaged human 26S proteasome with Nub1/FAT10 bound to Rpn1
9MBP 2.75 Å, Substrate-engaged human 26S proteasome bound to midnolin with RPT1 at top of spiral…
9DLP 2.79 Å, Cryo-EM structure of human TREX-2 complex bound to DDX39B(UAP56)
9NKG 2.8 Å, Structure of substrate engaged MIDN-bound human 26S proteasome, EB-MIDN (Composite map)
9E8I 2.87 Å, Human proteasome in resting state conformation bound to TXNL1 in Forward conformation
9BV3 2.9 Å, M1B Midnolin-Proteasome
9E8H 2.9 Å, Human proteasome in resting state conformation bound to TXNL1 in backward conformation
9K4J 2.9 Å, Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state EA1.0
9NKF 2.9 Å, Structure of human substrate-free 26S proteasome in the presence of ATPgS and…

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