2b34

Structure of MAR1 Ribonuclease from Caenorhabditis elegans

Method: X-RAY DIFFRACTION

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

MAR1 Ribonuclease

Caenorhabditis elegans

UniProt Q20062

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 8	water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q20062_CAEEL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–199； UniProt 1–199 Author chain B； PDBConstruct 1–199； UniProt 1–199 Author chain C； PDBConstruct 1–199； UniProt 1–199 Author chain D； PDBConstruct 1–199； UniProt 1–199 Author chain E； PDBConstruct 1–199； UniProt 1–199 Author chain F； PDBConstruct 1–199； UniProt 1–199 Author chain G； PDBConstruct 1–199； UniProt 1–199 Author chain H； PDBConstruct 1–199； UniProt 1–199

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	2b34
Deposition date deposition_date	2005-09-19
Structure title title	Structure of MAR1 Ribonuclease from Caenorhabditis elegans
Keywords keywords	;Isochorismatase Family, Structural Genomics, PSI, Protein Structure Initiative, Southeast Collaboratory for Structural Genomics, SECSG, HYDROLASE ;; HYDROLASE
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.

2b34__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2b34__assembly_3__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2b34__assembly_3__model_1 | P(r) · Pending

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

Rg（Guinier）	36.25 Å
Rg (electron density)	35.56 Å
Total Rg	36.09 Å
Atom count	11856
Residues	1536
Excluded volume	214080 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2b34__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2b34__assembly_2__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2b34__assembly_3__model_1`	octameric （8）	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)

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6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d2b34a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.0 — automated matches

Domain ID domain_id	d2b34b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.0 — automated matches

Domain ID domain_id	d2b34c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.0 — automated matches

Domain ID domain_id	d2b34d_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.0 — automated matches

Domain ID domain_id	d2b34e_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.0 — automated matches

Domain ID domain_id	d2b34f_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.0 — automated matches

Domain ID domain_id	d2b34g_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.0 — automated matches

Domain ID domain_id	d2b34h_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.33 — Isochorismatase-like hydrolases
Superfamily Superfamily superfamily	c.33.1 — Isochorismatase-like hydrolases
Family Family family	c.33.1.0 — automated matches

CATH v4.4 (8 domains)

Domain ID domain_id	2b34A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

Domain ID domain_id	2b34B00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

Domain ID domain_id	2b34C00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

Domain ID domain_id	2b34D00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

Domain ID domain_id	2b34E00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

Domain ID domain_id	2b34F00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

Domain ID domain_id	2b34G00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

Domain ID domain_id	2b34H00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	850 — Isochorismatase-like

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Unit-cell length a length_a	89.545 Å
Unit-cell length b length_b	113.973 Å
Unit-cell length c length_c	151.322 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	32

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.141 Å
Low-resolution limit resolution_low	41.670 Å
R factor r_factor	0.2217
R_work r_work	0.2195
R_free r_free	0.2627

Description description	MAR1 Ribonuclease
Molecular weight formula_weight	21877.4 kDa
Source method src_method	man
Copy count entity_count	8

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	12463

Structure of MAR1 Ribonuclease from Caenorhabditis elegans

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

MAR1 Ribonuclease

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

2b34__assembly_3__model_1

2b34__assembly_3__model_1 | I(q)

2b34__assembly_3__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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Source organism organism	Caenorhabditis elegans
NCBI taxonomy ID ncbi_taxonomy_id	6239
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	607

Structure of MAR1 Ribonuclease from Caenorhabditis elegans

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

MAR1 Ribonuclease

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

2b34__assembly_3__model_1

2b34__assembly_3__model_1 | I(q)

2b34__assembly_3__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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)