3LQC: Oxidized XRCC1

X-ray crystal structure of oxidized XRCC1 bound to DNA pol beta Palm thumb domain. Determined by X-ray diffraction at 2.35 Å resolution. Released 28 Apr 2010.

Method: X-ray diffraction
Resolution: 2.35 Å
Organisms: Homo sapiens, Rattus norvegicus
Chains: 2
Atoms: 2,972
Mol. weight: 44.67 kDa
Ligands: CO3
Released: 28 Apr 2010

Explore 3LQC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3LQC contains 18 α-helices and 19 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: 7 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
β-strand	7-12	6	1
α-helix	17-25	9
α-helix	28-36	9
β-strand	42-53	12	1
β-strand	57-64	8	2
β-strand	67-73	7	1
α-helix	81-83	3
β-strand	85-92	8	1
α-helix	96-101	6
β-strand	108-111	4	2
α-helix	113-115	3
α-helix	118-121	4
β-strand	125-133	9	1
β-strand	143-150	8	2

Chain B: 11 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	150-151	2	3
α-helix	152-169	18
β-strand	174-177	4	4
α-helix	179-182	4
β-strand	187-188	2	3
β-strand	191-196	6	4
α-helix	205-206	2
α-helix	209-220	12
β-strand	224-230	7	4
β-strand	234-239	6	4
α-helix	248-252	5
β-strand	253-259	7	4
α-helix	262-264	3
α-helix	265-273	9
α-helix	276-288	13
β-strand	291-293	3	5
β-strand	298-300	3	5
β-strand	301	1	6
β-strand	307	1	6
α-helix	310-312	3
α-helix	316-322	7
α-helix	330-332	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA repair protein XRCC1	A	protein	189	Homo sapiens	P18887 (AlphaFold model)
DNA polymerase beta	B	protein	200	Rattus norvegicus	P06766 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3LQC_1 DNA repair protein XRCC1 (chains A)
MPEIRLRHVVSCSSQDSTHCAENLLKADTYRKWRAAKAGEKTISVVLQLEKEEQIHSVDI
GNDGSAFVEVLVGSSAGGAGEQDYEVLLVTSSFMSPSESRSGSNPNRVRMFGPDKLVRAA
AEKRWDRVKIVCSQPYSKDSPFGLSFVRFHSPPDKDEAEAPSQKVTVTKLGQFRVKEEDE
SANHHHHHH

Sequence of entity 2 (B), FASTA

>3LQC_2 DNA polymerase beta (chains B)
YFEDFEKRIPREEMLQMQDIVLNEVKKLDPEYIATVCGSFRRGAESSGDMDVLLTHPNFT
SESSKQPKLLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSENDENEYPHRRIDIRLIP
KDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIFD
YIQWRYREPKDRSEHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
CO3	Carbonate ion	C O3	1

Water and common crystallization additives (NA) are not listed.

Primary citation

Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity. Cuneo, M.J., London, R.E. Proc Natl Acad Sci U S A (2010) 107:6805-6810. DOI 10.1073/pnas.0914077107 · PubMed

Other PDB entries of the same protein (UniProt P18887 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2W3O 1.85 Å, Crystal structure of the human PNKP FHA domain in complex with an XRCC1-derived…
5W7X 2.0 Å, Crystal Structure of FHA domain of human APLF in complex with XRCC1 bisphospho peptide
5W7Y 2.1 Å, Crystal Structure of FHA domain of human APLF in complex with XRCC1 monophosphorylated…
5E6Q 2.31 Å, Importin alpha binding to XRCC1 NLS peptide
6WH1 2.4 Å, Structure of the complex of human DNA ligase III-alpha and XRCC1 BRCT domains
6WH2 2.41 Å, Structure of the C-terminal BRCT domain of human XRCC1
3K77 2.6 Å, X-ray crystal structure of XRCC1
3K75 2.95 Å, X-ray crystal structure of reduced XRCC1 bound to DNA pol beta catalytic domain
1CDZ 3.2 Å, Brct domain from DNA-repair protein XRCC1
1XNA NMR solution structure of the single-strand break repair protein XRCC1-N-terminal domain
1XNT NMR solution structure of the single-strand break repair protein XRCC1-N-terminal domain
2D8M Solution structure of the first BRCT domain of DNA-repair protein XRCC1

Browse structure collections

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