5EAY: Dna2 peptide

Crystal structure of a Dna2 peptide in complex with Rpa 70N. Determined by X-ray diffraction at 1.55 Å resolution. Released 18 Nov 2015.

Method: X-ray diffraction
Resolution: 1.55 Å
Organism: Homo sapiens
Chains: 8
Atoms: 3,933
Mol. weight: 58.5 kDa
Released: 18 Nov 2015

Explore 5EAY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5EAY contains 20 α-helices and 24 β-strands across 8 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.

Chains A, B and D: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
β-strand	24-33	10	1
β-strand	41-47	7	1
β-strand	51-58	8	1
α-helix	60-62	3
α-helix	63-67	5
β-strand	76-86	11	1
β-strand	92-103	12	1
α-helix	105-108	4
β-strand	116-117	2	1

Chain C: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	9-15	7
β-strand	24-33	10	3
β-strand	41-47	7	3
β-strand	51-58	8	3
α-helix	60-62	3
α-helix	63-67	5
β-strand	76-86	11	3
β-strand	92-103	12	3
α-helix	105-108	4
β-strand	116-117	2	3

Chains E and F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4

Chains G and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	7-11	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Replication protein A 70 kDa DNA-binding subunit	A, B, C, D	protein	118	Homo sapiens	P27694 (AlphaFold model)
DNA replication ATP-dependent helicase/nuclease DNA2	E, F, G, H	protein	13	Homo sapiens	P51530 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>5EAY_1 Replication protein A 70 kDa DNA-binding subunit (chains A, B, C, D)
GQLSEGAIAAIMQKGDTNIKPILQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQL
NPLVEEEQLSSNCVCQIHRFIVNTLKDGRRVVILMELEVLKSAEAVGVKIGNPVPYNE

Sequence of entity 2 (E, F, G, H), FASTA

>5EAY_2 DNA replication ATP-dependent helicase/nuclease DNA2 (chains E, F, G, H)
NELELLMEKSFWE

Primary citation

Dna2 nuclease-helicase structure, mechanism and regulation by Rpa. Zhou, C., Pourmal, S., Pavletich, N.P. Elife (2015) 4. DOI 10.7554/eLife.09832 · PubMed

Other PDB entries of the same protein (UniProt P27694 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4O0A 1.2 Å, Fragment-Based Discovery of a Potent Inhibitor of Replication Protein A Protein-Protein…
5E7N 1.21 Å, Crystal Structure of RPA70N in complex with VU0085636
4IPC 1.22 Å, Structure of the N-terminal domain of RPA70, E7R mutant
4R4T 1.28 Å, Crystal Structure of RPA70N in complex with 5-(4-((4-(5-carboxyfuran-2-yl)phenylthioamido…
5N8A 1.28 Å, Structure of RPA70N in complex with PrimPol (fragment 480-560)
4R4O 1.33 Å, Crystal structure of RPA70N in complex with 5-(4-((4-(5-carboxyfuran-2-yl)benzyl)carbamot…
4NB3 1.35 Å, Crystal structure of RPA70N in complex with a 3,4 dichlorophenylalanine ATRIP derived…
4R4Q 1.35 Å, Crystal structure of RPA70N in complex with 5-(3-((N-(4-(5-carboxyfuran-2-yl)benzyl)aceta…
4LUV 1.4 Å, Fragment-Based Discovery of a Potent Inhibitor of Replication Protein A Protein-Protein…
4R4C 1.4 Å, Structure of RPA70N in complex with 5-(4-((4-(5-carboxyfuran-2-yl)-2-chlorobenzamido)meth…
4R4I 1.4 Å, Structure of RPA70N in complex with 5-(4-((6-(5-carboxyfuran-2-yl)-1-thioxo-3,4-dihydrois…
8K00 1.4 Å, RPA70N-MRE11 fusion

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