6M14: BARD1 BRCT Mutant

Crystal Structure of the BARD1 BRCT Mutant. Determined by X-ray diffraction at 1.88 Å resolution. Released 24 Feb 2021.

Method: X-ray diffraction
Resolution: 1.88 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,734
Mol. weight: 48.33 kDa
Released: 24 Feb 2021

Explore 6M14 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6M14 contains 21 α-helices and 20 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: 11 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	571-574	4	3
α-helix	579-592	14
β-strand	595-597	3	3
β-strand	606-609	4	3
α-helix	618-625	8
β-strand	629-632	4	3
α-helix	634-642	9
α-helix	648-651	4
β-strand	652	1	3
α-helix	656-665	10
α-helix	668-670	3
β-strand	676-679	4	4
α-helix	688-697	10
β-strand	701-702	2	4
α-helix	709-711	3
α-helix	713-715	3
α-helix	729-731	3
β-strand	735-739	5	4
β-strand	751-752	2	4
β-strand	755-759	5	4
α-helix	760-769	10

Chain B: 10 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	571-574	4	1
α-helix	579-591	13
β-strand	595-596	2	1
β-strand	606-609	4	1
α-helix	618-625	8
β-strand	629-632	4	1
α-helix	634-642	9
α-helix	648-651	4
β-strand	652	1	1
α-helix	656-665	10
α-helix	668-670	3
β-strand	676-679	4	2
α-helix	688-697	10
β-strand	701-702	2	2
α-helix	712-716	5
α-helix	729-731	3
β-strand	735-739	5	2
β-strand	751-752	2	2
β-strand	755-759	5	2
α-helix	760-769	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
BRCA1-associated RING domain protein 1	A, B	protein	210	Homo sapiens	Q99728 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6M14_1 BRCA1-associated RING domain protein 1 (chains A, B)
GPLVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGDAVQSTLKCMLGILNG
CWILKFEWVKACLRRKVCEQEEKYEIPEGPRRSRLNREQLLPKLFDGCYFYLWGTFKHHP
KDNLIKLLTAGGGQILSRKPKPDSDVTQTINTVAYHARPDSDQRFCTQYIIYEDLCNYHP
ERVRQGKVWKAPSSWFIDCVMSFELLPLDS

Primary citation

BARD1 is an ATPase activating protein for OLA1. Chen, T., Yeh, H.W., Chen, P.P. et al. Biochim Biophys Acta Gen Subj (2022) 1866:130099-130099. DOI 10.1016/j.bbagen.2022.130099 · PubMed

Other PDB entries of the same protein (UniProt Q99728 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2NTE 1.9 Å, Crystal Structure of the BARD1 BRCT Domains
3C5R 2.0 Å, Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences
2R1Z 2.1 Å, Crystal Structure of the BARD1 BRCT Repeat
3FA2 2.2 Å, Crystal Structure of the BRCA1 Associated Ring Domain (BARD1) Tandem BRCT Domains
7LYC 2.94 Å, Cryo-EM structure of the human nucleosome core particle ubiquitylated at histone H2A…
7E8I 3.1 Å, Structural insight into BRCA1-BARD1 complex recruitment to damaged chromatin
7LYB 3.28 Å, Cryo-EM structure of the human nucleosome core particle in complex with BRCA1-BARD1-UbcH5c
8GRQ 3.87 Å, Cryo-EM structure of BRCA1/BARD1 bound to H2AK127-UbcH5c-Ub nucleosome
7JZV 3.9 Å, Cryo-EM structure of the BRCA1-UbcH5c/BARD1 E3-E2 module bound to a nucleosome
1JM7 Solution structure of the BRCA1/BARD1 RING-domain heterodimer

Browse structure collections

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