8BAH: Human Mre11-Nbs1 complex

Human Mre11-Nbs1 complex. Determined by electron microscopy at 4.13 Å resolution. Released 11 Jan 2023.

Method: Electron microscopy
Resolution: 4.13 Å
Organism: Homo sapiens
Chains: 3
Atoms: 6,874
Mol. weight: 253.31 kDa
Ligands: MN
Released: 11 Jan 2023

Explore 8BAH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8BAH contains 42 α-helices and 59 β-strands across 3 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: 19 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	3-7	5
β-strand	13-18	6	1
β-strand	23	1	2
α-helix	35-49	15
β-strand	54-57	4	1
β-strand	62	1	2
α-helix	69-83	15
β-strand	84	1	3
α-helix	87-89	3
β-strand	92-93	2	4
α-helix	97-100	4
α-helix	110-112	3
β-strand	116	1	5
β-strand	118	1	3
β-strand	122-124	3	1
α-helix	128-130	3
β-strand	133	1	6
β-strand	138	1	6
α-helix	140-147	8
β-strand	150-152	3	1
β-strand	162-164	3	7
β-strand	167-171	5	4
β-strand	174-181	8	4
α-helix	186-194	9
β-strand	198-200	3	7
β-strand	202-203	2	8
α-helix	207-209	3
β-strand	211-216	6	4
α-helix	231-233	3
β-strand	240-243	4	4
β-strand	250-255	6	4
β-strand	262-265	4	4
α-helix	276-279	4
α-helix	281-282	2
β-strand	283-290	8	1
β-strand	293-300	8	1
α-helix	305-306	2
β-strand	307-313	7	9
α-helix	314-316	3
α-helix	328-352	25
β-strand	362-368	7	9
α-helix	378-382	5
α-helix	383-385	3
α-helix	392-394	3
β-strand	396-399	4	9

Chain B: 21 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	4-7	4
β-strand	13-18	6	10
β-strand	19	1	11
α-helix	35-49	15
β-strand	54-57	4	10
α-helix	69-83	15
β-strand	84	1	12
α-helix	87-89	3
β-strand	92-93	2	13
β-strand	95	1	14
α-helix	97-101	5
α-helix	110-112	3
β-strand	116	1	5
β-strand	118	1	12
β-strand	122-124	3	10
α-helix	128-130	3
β-strand	133	1	15
β-strand	138	1	15
α-helix	140-147	8
β-strand	150-152	3	10
β-strand	162-163	2	16
α-helix	165-166	2
β-strand	167-171	5	13
β-strand	174-181	8	13
α-helix	186-194	9
β-strand	198-199	2	16
β-strand	201-203	3	17
α-helix	207-209	3
β-strand	211-216	6	13
α-helix	231-233	3
β-strand	240-243	4	13
β-strand	250-255	6	13
β-strand	262-265	4	13
β-strand	268	1	11
α-helix	276-279	4
α-helix	281-282	2
β-strand	283-290	8	10
β-strand	293-295	3	10
β-strand	298-300	3	10
α-helix	305-306	2
β-strand	307-313	7	18
α-helix	314-316	3
α-helix	328-351	24
β-strand	362-368	7	18
α-helix	375-377	3
α-helix	378-382	5
α-helix	383-385	3
α-helix	392-394	3
β-strand	396-399	4	18

Chain C: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	659-660	2	8
β-strand	665	1	19
β-strand	669	1	19
α-helix	690-692	3
β-strand	703	1	14
α-helix	705-707	3
β-strand	708-710	3	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Double-strand break repair protein MRE11	A, B	protein	738	Homo sapiens	P49959 (AlphaFold model)
Nibrin	C	protein	754	Homo sapiens	O60934 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8BAH_1 Double-strand break repair protein MRE11 (chains A, B)
MSTADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGD
LFHENKPSRKTLHTCLELLRKYCMGDRPVQFEILSDQSVNFGFSKFPWVNYQDGNLNISI
PVFSIHGNNDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLLQKGSTKIALYG
LGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDL
VIWGHEHECKIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIP
LHTVRQFFMEDIVLANHPDIFNPDNPKVTQAIQSFCLEKIEEMLENAERERLGNSHQPEK
PLVRLRVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFRHREQKEKTGEEINFGKLITK
PSEGTTLRVEDLVKQYFQTAEKNVQLSLLTERGMGEAVQEFVDKEEKDAIEELVKYQLEK
TQRFLKERHIDALEDKIDEEVRRFRETRQKNTNEEDDEVREAMTRARALRSQSEESASAF
SADDLMSIDLAEQMANDSDDSISAATNKGRGRGRGRRGGRGQNSASRGGSQRGRADTGLE
TSTRSRNSKTAVSASRNMSIIDAFKSTRQQPSRNVTTKNYSEVIEVDESDVEEDIFPTTS
KTDQRWSSTSSSKIMSQSQVSKGVDFESSEDDDDDPFMNTSSLRRNRRSGGSLEVLFQGP
DYKDDDDKGTDYKDDDDK

Sequence of entity 2 (C), FASTA

>8BAH_2 Nibrin (chains C)
MWKLLPAAGPAGGEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQT
DEIPVLTLKDNSKYGTFVNEEKMQNGFSRTLKSGDGITFGVFGSKFRIEYEPLVACSSCL
DVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEF
LKAVESKKQPPQIESFYPPLDEPSIGSKNVDLSGRQERKQIFKGKTFIFLNAKQHKKLSS
AVVFGGGEARLITEENEEEHNFFLAPGTCVVDTGITNSQTLIPDCQKKWIQSIMDMLQRQ
GLRPIPEAEIGLAVIFMTTKNYCDPQGHPSTGLKTTTPGPSLSQGVSVDEKLMPSAPVNT
TTYVADTESEQADTWDLSERPKEIKVSKMEQKFRMLSQDAPTVKESCKTSSNNNSMVSNT
LAKMRIPNYQLSPTKLPSINKSKDRASQQQQTNSIRNYFQPSTKKRERDEENQEMSSCKS
ARIETSCSLLEQTQPATPSLWKNKEQHLSENEPVDTNSDNNLFTDTDLKSIVKNSASKSH
AAEKLRSNKKREMDDVAIEDEVLEQLFKDTKPELEIDVKVQKQEEDVNVRKRPRMDIETN
DTFSDEAVPESSKISQENEIGKKRELKEDSLWSAKEISNNDKLQDDSEMLPKKLLLTEFR
SLVIKNSTSRNPSGINDDYGQLKNFKKFKKVTYPGAGKLPHIIGGSDLIAHHARKNTELE
EWLRQEMEVQNQHAKEESLADDLFRYNPYLKRRR

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	4

Primary citation

Cryo-EM structure of the Mre11-Rad50-Nbs1 complex reveals the molecular mechanism of scaffolding functions. Rotheneder, M., Stakyte, K., van de Logt, E. et al. Mol Cell (2023) 83:167-185.e9. DOI 10.1016/j.molcel.2022.12.003 · PubMed

Other PDB entries of the same protein (UniProt P49959 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8K00 1.4 Å, RPA70N-MRE11 fusion
9Q9K 2.59 Å, Cryo-EM structure of human Mre11-Rad50 (MR) complex bound to DNA and telomeric factor…
9Q9J 2.71 Å, Cryo-EM structure of human Mre11-Rad50-Nbs1 (MRN) complex bound to DNA and telomeric…
9Q9I 2.79 Å, Cryo-EM structure of human Mre11-Rad50-Nbs1 complex bound to DNA
9Q9M 2.81 Å, Cryo-EM structure of human Mre11-Rad50-Nbs1 (MRN) complex bound to DNA and telomeric…
3T1I 3.0 Å, Crystal Structure of Human Mre11: Understanding Tumorigenic Mutations
9Q9H 3.11 Å, Cryo-EM structure of human Mre11-Rad50 complex bound to DNA
9ULO 3.91 Å, Cryo-EM structure of Human Mre11-Nbs1 complex

Browse structure collections

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