SAXSdb — 3cmv

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

Protein recA

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	MAGNESIUM ION × 4 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	MAGNESIUM ION × 4 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	MAGNESIUM ION × 4 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	MAGNESIUM ION × 4 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4	Consistent with protein count
5	Protein monomer	Monomer	Protein 1	MAGNESIUM ION × 4 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4	Consistent with protein count
6	Protein monomer	Monomer	Protein 1	MAGNESIUM ION × 4 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4	Consistent with protein count
7	Protein monomer	Monomer	Protein 1	MAGNESIUM ION × 4 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4	Consistent with protein count
8	Protein monomer	Monomer	Protein 1	MAGNESIUM ION × 4 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RECA_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–309； UniProt 31–335 Author chain A； PDBConstruct 325–658； UniProt 2–335 Author chain A； PDBConstruct 674–1007； UniProt 2–335 Author chain A； PDBConstruct 1024–1357； UniProt 2–335 Author chain B； PDBConstruct 5–309； UniProt 31–335 Author chain B； PDBConstruct 325–658； UniProt 2–335 Author chain B； PDBConstruct 674–1007； UniProt 2–335 Author chain B； PDBConstruct 1024–1357； UniProt 2–335 Author chain C； PDBConstruct 5–309； UniProt 31–335 Author chain C； PDBConstruct 325–658； UniProt 2–335 Author chain C； PDBConstruct 674–1007； UniProt 2–335 Author chain C； PDBConstruct 1024–1357； UniProt 2–335 Author chain D； PDBConstruct 5–309； UniProt 31–335 Author chain D； PDBConstruct 325–658； UniProt 2–335 Author chain D； PDBConstruct 674–1007； UniProt 2–335 Author chain D； PDBConstruct 1024–1357； UniProt 2–335 Author chain E； PDBConstruct 5–309； UniProt 31–335 Author chain E； PDBConstruct 325–658； UniProt 2–335 Author chain E； PDBConstruct 674–1007； UniProt 2–335 Author chain E； PDBConstruct 1024–1357； UniProt 2–335 Author chain F； PDBConstruct 5–309； UniProt 31–335 Author chain F； PDBConstruct 325–658； UniProt 2–335 Author chain F； PDBConstruct 674–1007； UniProt 2–335 Author chain F； PDBConstruct 1024–1357； UniProt 2–335 Author chain G； PDBConstruct 5–309； UniProt 31–335 Author chain G； PDBConstruct 325–658； UniProt 2–335 Author chain G； PDBConstruct 674–1007； UniProt 2–335 Author chain G； PDBConstruct 1024–1357； UniProt 2–335 Author chain H； PDBConstruct 5–309； UniProt 31–335 Author chain H； PDBConstruct 325–658； UniProt 2–335 Author chain H； PDBConstruct 674–1007； UniProt 2–335 Author chain H； PDBConstruct 1024–1357； UniProt 2–335

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	3cmv
Deposition date deposition_date	2008-03-24
Structure title title	Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
Keywords keywords	homologous recombination, recombination; RECOMBINATION
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.

3cmv__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3cmv__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3cmv__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	39.98 Å
Rg (electron density)	39.98 Å
Total Rg	40.18 Å
Atom count	8897
Residues	1163
Excluded volume	159380 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3cmv__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3cmv__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3cmv__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3cmv__assembly_4__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`3cmv__assembly_5__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`3cmv__assembly_6__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`3cmv__assembly_7__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`3cmv__assembly_8__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 (3)

Entity 1 Entity 1 polymer

Description description	Protein recA
Molecular weight formula_weight	144942.4 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	71761

GAMHGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGKTCAFIDAEHALDPIYARKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAVKEGENVVGSETRVKVVKNKIAAPFKQAEFQILYGEGINFYGELVDLGVKEKLIEKAGAWYSYKGEKIGQGKANATAWLKDNPETAKEIEKKVRELLLSNPNSTTGSTGSGTTGSTGSMAIDENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGKTCAFIDAEHALDPIYARKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAVKEGENVVGSETRVKVVKNKIAAPFKQAEFQILYGEGINFYGELVDLGVKEKLIEKAGAWYSYKGEKIGQGKANATAWLKDNPETAKEIEKKVRELLLSNPNSTTGSTGSMGHTTGSMSAIDENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGKTCAFIDAEHALDPIYARKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAVKEGENVVGSETRVKVVKNKIAAPFKQAEFQILYGEGINFYGELVDLGVKEKLIEKAGAWYSYKGEKIGQGKANATAWLKDNPETAKEIEKKVRELLLSNPNSTTGSTGSASGSSTGSMSAIDENKQKALAAALGQIEKQFGKGSIMRLGEDRSMDVETISTGSLSLDIALGAGGLPMGRIVEIYGPESSGKTTLTLQVIAAAQREGKTCAFIDAEHALDPIYARKLGVDIDNLLCSQPDTGEQALEICDALARSGAVDVIVVDSVAALTPKAEIEGEIGDSHMGLAARMMSQAMRKLAGNLKQSNTLLIFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRIGAVKEGENVVGSETRVKVVKNKIAAPFKQAEFQILYGEGINFYGELVDLGVKEKLIEKAGAWYSYKGEKIGQGKANATAWLKDNPETAKEIEKKVRELLLSNPNST

Source Source

Source organism organism

Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	32

Entity 3 Entity 3 non-polymer

Description description	PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
Molecular weight formula_weight	506.2 kDa
Source method src_method	syn
Copy count entity_count	32

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Unit-cell length a length_a	176.600 Å
Unit-cell length b length_b	189.800 Å
Unit-cell length c length_c	424.300 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	4.300 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2435
R_work r_work	0.2431
R_free r_free	0.2614

Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures

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

Protein recA

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

3cmv__assembly_2__model_1

3cmv__assembly_2__model_1 | I(q)

3cmv__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

7. Citations (1)

Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures

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

Protein recA

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

3cmv__assembly_2__model_1

3cmv__assembly_2__model_1 | I(q)

3cmv__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

7. Citations (1)