5W2L: Central domain of human Ctc1

Structure of a central domain of human Ctc1. Determined by X-ray diffraction at 1.86 Å resolution. Released 29 Nov 2017.

Method: X-ray diffraction
Resolution: 1.86 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,347
Mol. weight: 38.08 kDa
Ligands: HG
Released: 29 Nov 2017

Explore 5W2L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5W2L contains 14 α-helices and 24 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, 12 β-strands

Element	Residues	Length	Sheet
β-strand	728-738	11	1
β-strand	742-744	3	1
β-strand	746	1	2
α-helix	757-759	3
β-strand	760-769	10	1
β-strand	774-775	2	1
β-strand	776-777	2	3
β-strand	780-781	2	3
α-helix	783-786	4
β-strand	795-801	7	1
α-helix	802-810	9
β-strand	816-822	7	1
β-strand	842	1	2
α-helix	843-845	3
β-strand	851-853	3	1
α-helix	854-855	2
β-strand	859-862	4	1
α-helix	863-864	2
α-helix	865-873	9

Chain B: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	728-738	11	4
β-strand	742-744	3	4
β-strand	746	1	5
α-helix	747-749	3
α-helix	756-759	4
β-strand	760-769	10	4
β-strand	774-775	2	4
β-strand	776-777	2	6
β-strand	780-781	2	6
β-strand	795-801	7	4
α-helix	802-810	9
β-strand	816-822	7	4
β-strand	842	1	5
α-helix	843-845	3
β-strand	851-853	3	4
α-helix	854-855	2
β-strand	859-862	4	4
α-helix	863-864	2
α-helix	865-873	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
CST complex subunit CTC1	A, B	protein	168	Homo sapiens	Q2NKJ3 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5W2L_1 CST complex subunit CTC1 (chains A, B)
SNAQTDPTGPEGPHLGQSRLFLLCHKEALMKRNFCVPPGASPEVPKPALSFYVLGSWLGG
TQRKEGTGWGLPEPQGNDDNDQKVHLIFFGSSVRWFEFLHPGQVYRLIAPGPATPMLFEK
DGSSCISRRPLELAGCASCLTVQDNWTLELESSQDIQDVLDANKSLPE

Ligands and cofactors

ID	Name	Formula	Copies
HG	Mercury (II) ion	Hg	6

Primary citation

Structural and functional analysis of an OB-fold in human Ctc1 implicated in telomere maintenance and bone marrow syndromes. Shastrula, P.K., Rice, C.T., Wang, Z. et al. Nucleic Acids Res (2018) 46:972-984. DOI 10.1093/nar/gkx1213 · PubMed

Other PDB entries of the same protein (UniProt Q2NKJ3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6W6W 3.0 Å, Cryo-EM structure of CST bound to telomeric single-stranded DNA
8D0B 3.43 Å, Human CST-DNA polymerase alpha/primase preinitiation complex bound to 4xTEL-foldback…
8SOJ 3.8 Å, Cryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the absence of telomeric ssDNA
8SOK 4.1 Å, Cryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the presence of telomeric ssDNA
8D0K 4.27 Å, Human CST-DNA polymerase alpha/primase preinitiation complex bound to 4xTEL-foldback…
7U5C 4.6 Å, Cryo-EM structure of human CST bound to DNA polymerase alpha-primase in a recruitment…

Browse structure collections

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