5H65: Human POT1 and TPP1

Crystal structure of human POT1 and TPP1. Determined by X-ray diffraction at 2.1 Å resolution. Released 31 May 2017.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,815
Mol. weight: 38.81 kDa
Ligands: ZN
Released: 31 May 2017

Explore 5H65 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5H65 contains 20 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: 16 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	348-352	5
α-helix	355	1
β-strand	359-370	12	1
α-helix	374-377	4
β-strand	378-381	4	1
β-strand	388-390	3	1
α-helix	391-393	3
α-helix	394-404	11
α-helix	408-410	3
α-helix	411-413	3
β-strand	419-425	7	2
β-strand	433-439	7	2
α-helix	440	1
β-strand	441	1	3
β-strand	444	1	3
α-helix	448-450	3
β-strand	452-456	5	2
α-helix	460-469	10
β-strand	472-475	4	2
β-strand	476-478	3	4
β-strand	483-485	3	4
β-strand	493-495	3	2
β-strand	498-500	3	2
β-strand	502	1	5
α-helix	512-517	6
α-helix	526-532	7
β-strand	537	1	5
β-strand	539-549	11	1
β-strand	554-561	8	1
α-helix	570-573	4
α-helix	577-590	14
α-helix	597-599	3
α-helix	601-602	2
β-strand	603-611	9	1
β-strand	620-625	6	1

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	265-278	14
α-helix	286-289	4
α-helix	292-299	8
α-helix	310-312	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protection of telomeres protein 1	A	protein	294	Homo sapiens	Q9NUX5 (AlphaFold model)
Adrenocortical dysplasia protein homolog	B	protein	53	Homo sapiens	Q96AP0 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5H65_1 Protection of telomeres protein 1 (chains A)
QYLERTPLCAILKQKAPQQYRIRAKLRSYKPRRLFQSVKLHCPKCHLLQEVPHEGDLDII
FQDGATKTPDVKLQNTSLYDSKIWTTKNQKGRKVAVHFVKNNGILPLSNECLLLIEGGTL
SEICKLSNKFNSVIPVRSGHEDLELLDLSAPFLIQGTIHHYGCKQCSSLRSIQNLNSLVD
KTSWIPSSVAEALGIVPLQYVFVMTFTLDDGTGVLEAYLMDSDKFFQIPASEVLMDDDLQ
KSVDMIMDMFCPPGIKIDAYPWLECFIKSYNVTNGTDNQICYQIFDTTVAEDVI

Sequence of entity 2 (B), FASTA

>5H65_2 Adrenocortical dysplasia protein homolog (chains B)
GSEHQGALVCLAESCLTLEGPCTAPPVTHWAASRCKATGEAVYTVPSSMLCIS

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Primary citation

Structural insights into POT1-TPP1 interaction and POT1 C-terminal mutations in human cancer. Chen, C., Gu, P., Wu, J. et al. Nat Commun (2017) 8:14929-14929. DOI 10.1038/ncomms14929 · PubMed

Other PDB entries of the same protein (UniProt Q9NUX5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1XJV 1.73 Å, Crystal structure of human POT1 bound to telomeric single-stranded DNA (TTAGGGTTAG)
3KJO 1.8 Å, Crystal Structure of hPOT1V2-dTrUd(AGGGTTAG)
3KJP 1.8 Å, Crystal Structure of hPOT1V2-GGTTAGGGTTAG
5UN7 2.1 Å, Structure of the human POT1-TPP1 telomeric complex
8SH0 2.16 Å, Structure of human POT1 DNA binding domain bound to a 5'-phosphorylated junction of a…
7S1O 2.55 Å, Structure of human POT1C
7S1U 2.55 Å, Structure of human POT1C
8SH1 2.6 Å, Structure of human POT1 DNA binding domain bound to a 5'-phosphorylated junction of a…
7S1T 2.9 Å, Structure of the human POT1-TPP1 complex
8SOJ 3.8 Å, Cryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the absence of telomeric ssDNA
7QXB 3.9 Å, Cryo-EM map of human telomerase-DNA-TPP1-POT1 complex (sharpened map)
7QXS 3.9 Å, Cryo-EM structure of human telomerase-DNA-TPP1-POT1 complex (with POT1 side chains)

Browse structure collections

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