4Z0U: RNase HI/SSB-Ct complex

RNase HI/SSB-Ct complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 29 Apr 2015.

Method: X-ray diffraction
Resolution: 2.0 Å
Organisms: Escherichia coli O139:H28, Escherichia coli
Chains: 4
Atoms: 2,703
Mol. weight: 37.85 kDa
Released: 29 Apr 2015

Explore 4Z0U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4Z0U contains 16 α-helices and 16 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: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	4-13	10	1
β-strand	18-28	11	1
β-strand	31-42	12	1
α-helix	44-57	14
β-strand	64-69	6	1
α-helix	72-76	5
α-helix	77-81	5
α-helix	82-88	7
β-strand	91	1	2
β-strand	97	1	2
α-helix	98	1
α-helix	101-111	11
β-strand	115-120	6	1
α-helix	128-141	14
β-strand	146	1	1

Chain B: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	2	1
β-strand	3-13	11	3
β-strand	18-28	11	3
β-strand	31-42	12	3
α-helix	44-57	14
β-strand	63-69	7	3
α-helix	72-76	5
α-helix	77-81	5
α-helix	82-87	6
β-strand	91	1	4
β-strand	97	1	4
α-helix	98	1
α-helix	101-111	11
β-strand	115-120	6	3
α-helix	128-141	14
β-strand	146	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ribonuclease H	A, B	protein	155	Escherichia coli O139:H28	A7ZHV1 (AlphaFold model)
SSB-Ct Peptide	D, E	protein	10	Escherichia coli	P0AGE0 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4Z0U_1 Ribonuclease H (chains A, B)
MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALK
EHCEVILSTDSQYVRQGITQWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEW
VKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV

Sequence of entity 2 (D, E), FASTA

>4Z0U_2 SSB-Ct Peptide (chains D, E)
WMDFDDDIPF

Primary citation

Interaction with Single-stranded DNA-binding Protein Stimulates Escherichia coli Ribonuclease HI Enzymatic Activity. Petzold, C., Marceau, A.H., Miller, K.H. et al. J Biol Chem (2015) 290:14626-14636. DOI 10.1074/jbc.M115.655134 · PubMed

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