SAXSdb — 5a6s

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

ENDOLYSIN

CLOSTRIDIUM PHAGE PHICTP1

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	SULFATE ION × 2 GLYCEROL × 6 PENTAETHYLENE GLYCOL × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D9ZNF3_9CAUD
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 21–294； UniProt 1–274 Author chain B； PDBConstruct 1–80； UniProt 195–274

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	5a6s
Deposition date deposition_date	2015-07-01
Structure title title	Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product
Keywords keywords	STRUCTURAL PROTEIN, ENDOLYSIN, SECONDARY TRANSLATION PRODUCT, BACTERIOPHAGE; STRUCTURAL PROTEIN
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.

5a6s__assembly_1__model_1

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

Download this curve (.dat)

5a6s__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5a6s__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	37.19 Å
Rg (electron density)	38.20 Å
Total Rg	38.16 Å
Atom count	5638
Residues	708
Excluded volume	100720 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5a6s__assembly_1__model_1`	tetrameric （4）	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 (6)

Entity 1 Entity 1 polymer

Description description	ENDOLYSIN
Molecular weight formula_weight	32877.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3299

MGSSHHHHHHSSGLVPRGSHMKKIADISNLNGNVDVKLLFNLGYIGIIAKASEGGTFVDKYYKQNYTNTKAQGKITGAYHFANFSTIAKAQQEANFFLNCIAGTTPDFVVLDLEQQCTGDITDACLAFLNIVAKKFKCVVYCNSSFIKEHLNSKICAYPLWIANYGVATPAFTLWTKYAMWQFTEKGQVSGISGYIDFSYITDEFIKYIKGEDEVENLVVYNDGADQRAAEYLADRLACPTINNARKFDYSNVKNVYAVGGNKEQYTSYLTTLIAGSTRYTTMQAVLDYIKNLK

Source Source

Source organism organism	CLOSTRIDIUM PHAGE PHICTP1
NCBI taxonomy ID ncbi_taxonomy_id	871584
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	ENDOLYSIN
Molecular weight formula_weight	9031.1 kDa
Mutation mutation	YES
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MENLVVYNDGADQRAAEYLADRLACPTINNARKFDYSNVKNVYAVGGNKEQYTSYLTTLIAGSTRYTTMQAVLDYIKNLK

Source Source

Source organism organism	CLOSTRIDIUM PHAGE PHICTP1
NCBI taxonomy ID ncbi_taxonomy_id	871584
Host organism host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 non-polymer

Description description	PENTAETHYLENE GLYCOL
Molecular weight formula_weight	238.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	480

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6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id	5a6sA01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	80 — Glycosidases

Domain ID domain_id	5a6sA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	12090 —

Domain ID domain_id	5a6sB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	12090 —

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Unit-cell length a length_a	136.197 Å
Unit-cell length b length_b	136.197 Å
Unit-cell length c length_c	56.457 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	19.900 Å
R factor r_factor	0.1641
R_work r_work	0.1620
R_free r_free	0.2047

Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product

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

ENDOLYSIN

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

5a6s__assembly_1__model_1

5a6s__assembly_1__model_1 | I(q)

5a6s__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

7. Citations (1)

Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product

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

ENDOLYSIN

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

5a6s__assembly_1__model_1

5a6s__assembly_1__model_1 | I(q)

5a6s__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

7. Citations (1)