7S1T: Human POT1-TPP1 complex

Structure of the human POT1-TPP1 complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 19 Jan 2022.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 8
Atoms: 11,776
Mol. weight: 181.41 kDa
Ligands: ZN
Released: 19 Jan 2022

Explore 7S1T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7S1T contains 83 α-helices and 100 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.

Chain A: 13 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	335-337	3	1
β-strand	345	1	1
α-helix	346-347	2
α-helix	348-352	5
β-strand	358-370	13	1
α-helix	374-376	3
β-strand	378-381	4	1
β-strand	388-390	3	1
α-helix	391-393	3
α-helix	394-404	11
β-strand	419-423	5	2
β-strand	427	1	3
β-strand	435-439	5	2
β-strand	441	1	4
β-strand	444	1	4
α-helix	448-450	3
β-strand	452-456	5	2
α-helix	460-467	8
β-strand	472-475	4	2
β-strand	476-478	3	5
β-strand	483-485	3	5
β-strand	493-495	3	2
β-strand	498-500	3	2
β-strand	502	1	6
α-helix	512-517	6
α-helix	526-533	8
β-strand	537	1	6
β-strand	539-549	11	1
β-strand	554-561	8	1
α-helix	573-575	3
α-helix	577-590	14
β-strand	593	1	7
β-strand	595	1	7
α-helix	597-599	3
α-helix	600-601	2
β-strand	602-612	11	1
β-strand	619-625	7	1
β-strand	627-629	3	1

Chain B: 4 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	254-259	6
α-helix	263-278	16
β-strand	282	1	3
α-helix	292-297	6
α-helix	317-323	7

Chain D: 16 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	335-337	3	8
α-helix	344-347	4
α-helix	348-352	5
α-helix	355	1
β-strand	359-360	2	9
β-strand	363-364	2	8
β-strand	365-370	6	9
α-helix	374-377	4
β-strand	378-381	4	9
β-strand	388-390	3	9
α-helix	391-393	3
α-helix	394-404	11
β-strand	419-423	5	10
β-strand	435-439	5	10
β-strand	441	1	11
β-strand	444	1	11
α-helix	448-450	3
β-strand	452-453	2	10
β-strand	456	1	10
α-helix	460-469	10
β-strand	472-473	2	10
β-strand	476	1	12
β-strand	485	1	12
β-strand	493-495	3	10
β-strand	498-500	3	10
β-strand	502	1	13
α-helix	509-511	3
α-helix	512-517	6
α-helix	526-533	8
β-strand	537	1	13
β-strand	539-549	11	9
β-strand	554-561	8	9
α-helix	573-575	3
α-helix	577-590	14
α-helix	597-599	3
α-helix	601-602	2
β-strand	603-604	2	8
β-strand	607-613	7	9
β-strand	618-624	7	9
β-strand	627-629	3	8
α-helix	630-631	2

Chain E: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	255-259	5
α-helix	263-276	14
α-helix	287-289	3
α-helix	292-296	5
α-helix	304-306	3
α-helix	310-312	3
α-helix	317-323	7

Chain G: 14 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	335-337	3	14
α-helix	348-352	5
β-strand	359-360	2	15
β-strand	363-364	2	14
β-strand	365-370	6	15
α-helix	374-376	3
β-strand	378-381	4	15
β-strand	388-390	3	15
α-helix	391-393	3
α-helix	394-404	11
β-strand	419-425	7	16
β-strand	433-439	7	16
β-strand	441	1	17
β-strand	444	1	17
α-helix	448-450	3
β-strand	452-456	5	16
α-helix	460-469	10
β-strand	472-478	7	16
β-strand	483-485	3	16
α-helix	486-487	2
β-strand	493-495	3	16
β-strand	498-500	3	16
β-strand	502	1	18
α-helix	512-517	6
α-helix	526-533	8
β-strand	537	1	18
α-helix	538	1
β-strand	539-549	11	15
β-strand	554-561	8	15
α-helix	573-575	3
α-helix	577-590	14
α-helix	597-599	3
α-helix	601-602	2
β-strand	603-604	2	14
β-strand	606-613	8	15
β-strand	618-625	8	15
β-strand	627-629	3	14

Chain H: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	255-260	6
α-helix	265-275	11
α-helix	287-289	3
α-helix	292-297	6
α-helix	304-306	3
α-helix	310-312	3
α-helix	317-322	6

Chain J: 14 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	335-337	3	19
β-strand	345	1	20
α-helix	348-351	4
β-strand	359-370	12	20
α-helix	374-376	3
β-strand	378-381	4	20
β-strand	388-390	3	20
α-helix	391-393	3
α-helix	394-403	10
β-strand	419-425	7	21
β-strand	427	1	22
β-strand	433-439	7	21
β-strand	441	1	23
β-strand	444	1	23
α-helix	448-450	3
β-strand	452-456	5	21
α-helix	460-469	10
β-strand	472-475	4	21
β-strand	476-478	3	24
β-strand	483-485	3	24
β-strand	493-495	3	21
β-strand	498-500	3	21
β-strand	502	1	25
α-helix	509-511	3
α-helix	512-517	6
α-helix	526-533	8
α-helix	535-536	2
β-strand	537	1	25
α-helix	538	1
β-strand	539-549	11	20
β-strand	555-561	7	20
α-helix	573-575	3
α-helix	577-590	14
β-strand	593	1	26
β-strand	595	1	26
α-helix	601	1
β-strand	602-612	11	20
β-strand	619-624	6	20
β-strand	627-629	3	19

Chain K: 8 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	256-260	5
α-helix	263-277	15
β-strand	282	1	22
α-helix	285-289	5
α-helix	292-297	6
α-helix	304-306	3
α-helix	310-312	3
α-helix	317-320	4
α-helix	322-324	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protection of telomeres protein 1	A, D, G, J	protein	313	Homo sapiens	Q9NUX5 (AlphaFold model)
Adrenocortical dysplasia protein homolog	B, E, H, K	protein	93	Homo sapiens	Q96AP0 (AlphaFold model)

Sequence of entity 1 (A, D, G, J), FASTA

>7S1T_1 Protection of telomeres protein 1 (chains A, D, G, J)
SNIEVERCQQLSATILTDHQYLERTPLCAILKQKAPQQYRIRAKLRSYKPRRLFQSVKLH
CPKCHLLQEVPHEGDLDIIFQDGATKTPDVKLQNTSLYDSKIWTTKNQKGRKVAVHFVKN
NGILPLSNECLLLIEGGTLSEICKLSNKFNSVIPVRSGHEDLELLDLSAPFLIQGTIHHY
GCKQCSSLRSIQNLNSLVDKTSWIPSSVAEALGIVPLQYVFVMTFTLDDGTGVLEAYLMD
SDKFFQIPASEVLMDDDLQKSVDMIMDMFCPPGIKIDAYPWLECFIKSYNVTNGTDNQIC
YQIFDTTVAEDVI

Sequence of entity 2 (B, E, H, K), FASTA

>7S1T_2 Adrenocortical dysplasia protein homolog (chains B, E, H, K)
STSSNAGLSLSQLLDEMREDQEHQGALVCLAESCLTLEGPCTAPPVTHWAASRCKATGEA
VYTVPSSMLCISENDQLILSSLGPCQRTQGPEL

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4

Primary citation

POT1-TPP1 binding stabilizes POT1, promoting efficient telomere maintenance. Aramburu, T., Kelich, J., Rice, C. et al. Comput Struct Biotechnol J (2022) 20:675-684. DOI 10.1016/j.csbj.2022.01.005 · 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
5H65 2.1 Å, Crystal structure of human POT1 and TPP1
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…
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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