SAXSdb — 3du5

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Telomerase reverse transcriptase

Tribolium castaneum

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q0QHL8_TRICA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–596； UniProt 1–596 Author chain B； PDBConstruct 1–596； UniProt 1–596

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3du5
Deposition date deposition_date	2008-07-16
Structure title title	Structure of the catalytic subunit of telomerase, TERT
Keywords keywords	Reverse Transcriptase, RNA-directed DNA polymerase, TRANSFERASE; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

3du5__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3du5__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3du5__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	29.35 Å
Rg (electron density)	28.38 Å
Total Rg	29.24 Å
Atom count	4982
Residues	596
Excluded volume	90380 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3du5__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3du5__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Telomerase reverse transcriptase
Molecular weight formula_weight	70588.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	10041

MVHYYRLSLKSRQKAPKIVNSKYNSILNIALKNFRLCKKHKTKKPVQILALLQEIIPKSYFGTTTNLKRFYKVVEKILTQSSFECIHLSVLHKCYDYDAIPWLQNVEPNLRPKLLLKHNLFLLDNIVKPIIAFYYKPIKTLNGHEIKFIRKEEYISFESKVFHKLKKMKYLVEVQDEVKPRGVLNIIPKQDNFRAIVSIFPDSARKPFFKLLTSKIYKVLEEKYKTSGSLYTCWSEFTQKTQGQIYGIKVDIRDAYGNVKIPVLCKLIQSIPTHLLDSEKKNFIVDHISNQFVAFRRKIYKWNHGLLQGDPLSGCLCELYMAFMDRLYFSNLDKDAFIHRTVDDYFFCSPHPHKVYDFELLIKGVYQVNPTKTRTNLPTHRHPQDEIPYCGKIFNLTTRQVRTLYKLPPNYEIRHKFKLWNFNNQISDDNPARFLQKAMDFPFICNSFTKFEFNTVFNDQRTVFANFYDAMICVAYKFDAAMMALRTSFLVNDFGFIWLVLSSTVRAYASRAFKKIVTYKGGKYRKVTFQCLKSIAWRAFLAVLKRRTEIYKGLIDRIKSREKLTMKFHDGEVDASYFCKLPEKFRFVKINRKASI

Source Source

Source organism organism	Tribolium castaneum
Common name common_name	Red flour beetle
NCBI taxonomy ID ncbi_taxonomy_id	7070
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	77

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6. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id	3du5A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	132 — Topoisomerase I; Chain A, domain 4
Homologous superfamily homologous superfamily	70 —

Domain ID domain_id	3du5A02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	10 — HIV Type 1 Reverse Transcriptase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3du5A03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	2210 —

Domain ID domain_id	3du5A04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	2630 —

Domain ID domain_id	3du5A05
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	357 — Tetracycline Repressor; domain 2
Homologous superfamily homologous superfamily	90 — Telomerase reverse transcriptase (TERT), thumb domain

Domain ID domain_id	3du5B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	132 — Topoisomerase I; Chain A, domain 4
Homologous superfamily homologous superfamily	70 —

Domain ID domain_id	3du5B02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	10 — HIV Type 1 Reverse Transcriptase; Chain A, domain 1
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3du5B03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	2210 —

Domain ID domain_id	3du5B04
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	2630 —

Domain ID domain_id	3du5B05
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	357 — Tetracycline Repressor; domain 2
Homologous superfamily homologous superfamily	90 — Telomerase reverse transcriptase (TERT), thumb domain

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Unit-cell length a length_a	199.968 Å
Unit-cell length b length_b	199.968 Å
Unit-cell length c length_c	96.413 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 61
Space-group number int_tables_number	169
Crystal system crystal_system	—

Resolution resolution	3.250 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2460
R_work r_work	0.2433
R_free r_free	0.2965

Structure of the catalytic subunit of telomerase, TERT

1. Protein Identity and Related Structures Protein Identity & Related Structures

Telomerase reverse transcriptase

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3du5__assembly_1__model_1

3du5__assembly_1__model_1 | I(q)

3du5__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

7. Citations (1)

Structure of the catalytic subunit of telomerase, TERT

1. Protein Identity and Related Structures Protein Identity & Related Structures

Telomerase reverse transcriptase

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3du5__assembly_1__model_1

3du5__assembly_1__model_1 | I(q)

3du5__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

7. Citations (1)