SAXSdb — 4psv

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

Protein RecA, 1st part, 2nd part

Mycobacterium tuberculosis

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RECA_MYCTU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–251； UniProt 1–251 Author chain A； PDBConstruct 252–350； UniProt 692–790

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	4psv
Deposition date deposition_date	2014-03-08
Structure title title	Mycobacterium tuberculosis RecA phosphate bound room temperature structure I-RT
Keywords keywords	;HOMOLOGOUS RECOMBINATION, DNA REPAIR, ATPASE, RECOMBINASE, DNA BINDING PROTEIN, PLOOP CONTAINING NTPASE FOLD, ATP BINDING, HYDROLYSIS, 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.

4psv__assembly_1__model_1

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

Download this curve (.dat)

4psv__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4psv__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	21.96 Å
Rg (electron density)	20.79 Å
Total Rg	21.58 Å
Atom count	2255
Residues	311
Excluded volume	39986 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4psv__assembly_1__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, 1st part, 2nd part
Molecular weight formula_weight	37222.2 kDa
EC 编号 ec_number	3.1.-.-
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	2312

MTQTPDREKALELAVAQIEKSYGKGSVMRLGDEARQPISVIPTGSIALDVALGIGGLPRGRVIEIYGPESSGKTTVALHAVANAQAAGGVAAFIDAEHALDPDYAKKLGVDTDSLLVSQPDTGEQALEIADMLIRSGALDIVVIDSVAALVPRAELEGEMGDSHVGLQARLMSQALRKMTGALNNSGTTAIFINQLRDKIGVMFGSPETTTGGKALKFYASVRMDVRRVETLKDGTNAVGNRTRVKVVKNKCSPPFKQAEFDILYGKGISREGSLIDMGVDQGLIRKSGAWFTYEGEQLGQGKENARNFLVENADVADEIEKKIKEKLGIGAVVTDDPSNDGVLPAPVDF

Source Source

Source organism organism	Mycobacterium tuberculosis
NCBI taxonomy ID ncbi_taxonomy_id	1773
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	51

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d4psva1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.11 — RecA protein-like (ATPase-domain)

Domain ID domain_id	d4psva2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.48 — Anti-LPS factor/recA domain
Superfamily Superfamily superfamily	d.48.1 — RecA protein, C-terminal domain
Family Family family	d.48.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	4psvA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	4psvA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	250 — Rec A Protein; domain 2
Homologous superfamily homologous superfamily	10 — RecA protein, C-terminal domain

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7. Citations (6)

Structural studies on Mycobacterium tuberculosis RecA: Molecular plasticity and interspecies variability

J.Biosci. (2015)

PMID: 25740138 · DOI: 10.1007/s12038-014-9497-x PRIMARY

Functionally important movements in RecA molecules and filaments: studies involving mutation and environmental changes

Acta Crystallogr.,Sect.D (2008)

PMID: 19020353 · DOI: 10.1107/S0907444908028448

;Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery ;

Nucleic Acids Res. (2006)

PMID: 16648362 · DOI: 10.1093/nar/gkl107

Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes

J.Bacteriol. (2003)

PMID: 12837805 · DOI: 10.1128/JB.185.14.4280-4284.2003

;Structural studies on MtRecA-nucleotide complexes: insights into DNA and nucleotide binding and the structural signature of NTP recognition ;

Proteins (2003)

PMID: 12557189 · DOI: 10.1002/prot.10315

;Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): implications for decreased ATPase activity and molecular aggregation ;

Nucleic Acids Res. (2000)

PMID: 11121488 · DOI: 10.1093/nar/28.24.4964

Unit-cell length a length_a	108.416 Å
Unit-cell length b length_b	108.416 Å
Unit-cell length c length_c	72.748 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	6

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

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	27.110 Å
R factor r_factor	0.1583
R_work r_work	0.1541
R_free r_free	0.1959

Mycobacterium tuberculosis RecA phosphate bound room temperature structure I-RT

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

Protein RecA, 1st part, 2nd part

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

4psv__assembly_1__model_1

4psv__assembly_1__model_1 | I(q)

4psv__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (6)

Mycobacterium tuberculosis RecA phosphate bound room temperature structure I-RT

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

Protein RecA, 1st part, 2nd part

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

4psv__assembly_1__model_1

4psv__assembly_1__model_1 | I(q)

4psv__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (6)