SAXSdb — 2zjb

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

Meiotic recombination protein DMC1/LIM15 homolog

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 1–340 Chain B； UniProt 1–340	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；0.1M sodium citrate, 50mM MgCl2, 8% PEG 2000 MME, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.50 Å R-free 0.351

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 2ZJB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1V5W Crystal structure of the human Dmc1 protein Deposited 2003-11-26	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–340（340 aa） Chain B 1–340（340 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；PEG2000MME, Magnesium chloride, Sodium citrate, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.346
1V5W Crystal structure of the human Dmc1 protein Deposited 2003-11-26	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–340（340 aa） Chain B 1–340（340 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；PEG2000MME, Magnesium chloride, Sodium citrate, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.346
4HYY Filament of octameric rings of DMC1 recombinase from Homo sapiens Deposited 2012-11-14	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 84–340（257 aa） Fragment：ATPase domain Chain B 84–340（257 aa） Fragment：ATPase domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；294 K；6% PEG 3350, 0.5 M NaCl, 0.05 M MgCl2, 0.05 M HEPES-NACl, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 2.60 Å R-free 0.246
4HYY Filament of octameric rings of DMC1 recombinase from Homo sapiens Deposited 2012-11-14	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain C 84–340（257 aa） Fragment：ATPase domain Chain D 84–340（257 aa） Fragment：ATPase domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；294 K；6% PEG 3350, 0.5 M NaCl, 0.05 M MgCl2, 0.05 M HEPES-NACl, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 2.60 Å R-free 0.246
4HYY Filament of octameric rings of DMC1 recombinase from Homo sapiens Deposited 2012-11-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 84–340（257 aa） Fragment：ATPase domain Chain B 84–340（257 aa） Fragment：ATPase domain Chain C 84–340（257 aa） Fragment：ATPase domain Chain D 84–340（257 aa） Fragment：ATPase domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；294 K；6% PEG 3350, 0.5 M NaCl, 0.05 M MgCl2, 0.05 M HEPES-NACl, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 294.0K	Resolution 2.60 Å R-free 0.246
6R3P Crystal structure of human DMC1 ATPase domain Deposited 2019-03-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 83–340（258 aa） Chain B 83–340（258 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；293 K；50 mM HEPES-NaOH pH 7.2, 50 mM MgCl2, 500 mM NaCl, 7.5 % PEG3350	Resolution 2.05 Å R-free 0.219
6R3P Crystal structure of human DMC1 ATPase domain Deposited 2019-03-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain C 83–340（258 aa） Chain D 83–340（258 aa）	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 8 PG4 TETRAETHYLENE GLYCOL × 4 P6G HEXAETHYLENE GLYCOL × 8 1PE PENTAETHYLENE GLYCOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；293 K；50 mM HEPES-NaOH pH 7.2, 50 mM MgCl2, 500 mM NaCl, 7.5 % PEG3350	Resolution 2.05 Å R-free 0.219
7C98 Human DMC1 post-synaptic complexes Deposited 2020-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: pentameric	Chain A 1–340（340 aa） Chain B 1–340（340 aa） Chain C 1–340（340 aa）	Not recorded	CA CALCIUM ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25 mM Tris-HCl, pH 7.5, 50 mM KCl and 1 mM dithiothreitol) containing 2 mM AMP-PNP and 5 mM CaCl2 cryo-EM vitrification conditions Cryogen ETHANE；The grids were blotted for 1 sec at 22 degree C with 100% relative humidity and plunge-frozen in liquid ethane cooled by liquid nitrogen using a Vitrobot Mark IV (Thermo Fisher).	Resolution 3.47 Å
7C99 Human DMC1 post-synaptic complexes with mismatched dsDNA Deposited 2020-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: pentameric	Chain A 1–340（340 aa） Chain B 1–340（340 aa） Chain C 1–340（340 aa）	Not recorded	CA CALCIUM ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25 mM Tris-HCl, pH 7.5, 50 mM KCl and 1 mM dithiothreitol) containing 2 mM AMP-PNP and 5 mM CaCl2 cryo-EM vitrification conditions Cryogen ETHANE；The grids were blotted for 1 sec at 22 degree C with 100% relative humidity and plunge-frozen in liquid ethane cooled by liquid nitrogen using a Vitrobot Mark IV (Thermo Fisher).	Resolution 3.36 Å
7C9C Human DMC1 pre-synaptic complexes Deposited 2020-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: tetrameric	Chain A 1–340（340 aa） Chain B 1–340（340 aa） Chain C 1–340（340 aa）	Not recorded	CA CALCIUM ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25 mM Tris-HCl, pH 7.5, 50 mM KCl and 1 mM dithiothreitol) containing 2 mM AMP-PNP and 5 mM CaCl2 cryo-EM vitrification conditions Cryogen ETHANE；The grids were blotted for 1 sec at 22 degree C with 100% relative humidity and plunge-frozen in liquid ethane cooled by liquid nitrogen using a Vitrobot Mark IV (Thermo Fisher).	Resolution 3.33 Å
7CGY Human DMC1 Q244M mutant of the post-synaptic complexes Deposited 2020-07-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–340（340 aa） Chain B 1–340（340 aa） Chain C 1–340（340 aa）	Mutation：Q244M Mutation：Q244M Mutation：Q244M	CA CALCIUM ION × 3 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25 mM Tris-HCl, pH 7.5, 50 mM KCl and 1 mM dithiothreitol) containing 2 mM AMP-PNP and 5 mM CaCl2 cryo-EM vitrification conditions Cryogen ETHANE；The grids were blotted for 1 sec at 22 degree C with 100% relative humidity and plunge-frozen in liquid ethane cooled by liquid nitrogen using a Vitrobot Mark IV (Thermo Fisher).	Resolution 3.20 Å
8QQE Crystal structure of the complex between DMC1 and the PhePP domain of BRCA2 Deposited 2023-10-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain A 2–340（339 aa） Chain B 2–340（339 aa）	Not recorded	MG MAGNESIUM ION × 4 CL CHLORIDE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6；293 K；0.1M MES at pH 6, 2.4 M sodium formate	Resolution 3.46 Å R-free 0.261
8R2G Crystal structure of a BRCA2-DMC1 complex Deposited 2023-11-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain A 83–340（258 aa） Chain B 83–340（258 aa） Chain C 83–340（258 aa） Chain D 83–340（258 aa） Chain E 83–340（258 aa） Chain F 83–340（258 aa） Chain G 83–340（258 aa） Chain H 83–340（258 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；50 mM HEPES-NaOH pH 7.4, 50 mM MgCl2, 500 mM NaCl, 8 % PEG 3350, 20 % glycerol	Resolution 3.45 Å R-free 0.306

9 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	DMC1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–343； UniProt 1–340 Author chain B； PDBConstruct 4–343； UniProt 1–340

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	2zjb
Deposition date deposition_date	2008-03-02
Structure title title	Crystal structure of the human Dmc1-M200V polymorphic variant
Keywords keywords	;DNA-BINDING PROTEIN, RING PROTEIN, OCTAMER, AAA ATPASE, ATP-binding, Cell cycle, Meiosis, Nucleotide-binding, Nucleus, Polymorphism, RECOMBINATION ;; RECOMBINATION
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	25.09 Å
Radius of gyration Rg (electron density) rg_electron	24.12 Å
Forward intensity I(0) i0	47224200.00
Molecular weight molecular_weight	53183.0 kDa
Excluded volume excluded_volume	66596 Å³
Envelope volume envelope_volume	80912 Å³
Hydration-shell volume shell_volume	27934 Å³
Envelope diameter envelope_diameter	89.1 Å
Shell Rg shell_rg	31.21 Å
Envelope Rg envelope_rg	24.48 Å
Shape Rg shape_rg	24.14 Å
Total Rg total_rg	24.89 Å
Total atoms total_atoms	3748
Residues n_residues	478
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	86.5 Å
Rg (real space) rg_real	25.09 Å
Rg uncertainty (real space) rg_real_error	0.63 Å
I(0) (real space) i0_real	4.7220e+07
I(0) uncertainty (real space) i0_real_error	6.8870e+05
Rg (reciprocal space) rg_reciprocal	25.09 Å
I(0) (reciprocal space) i0_reciprocal	47220000.0000
Solution quality estimate total_estimate	0.8621
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	28.8 Å
Skewness Skewness skewness	0.383
Kurtosis Kurtosis kurtosis	-0.226
Angular range angular_range	— – 0.3150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12880000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.772; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.934

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	2zjbA00
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	2zjbB00
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

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8. Citations (1)

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Unit-cell length a length_a	124.089 Å
Unit-cell length b length_b	124.089 Å
Unit-cell length c length_c	217.870 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	I 4 2 2
Space-group number int_tables_number	97
Crystal system crystal_system	—

Resolution resolution	3.500 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.2940
R_free r_free	0.3510

Description description	Meiotic recombination protein DMC1/LIM15 homolog
Molecular weight formula_weight	37981.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3748

Crystal structure of the human Dmc1-M200V polymorphic variant

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

Meiotic recombination protein DMC1/LIM15 homolog

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

fit	/app/data/saxs_computation/zj/2zjb/2zjb.fit
pddf	/app/data/pr_computation/zj/2zjb/2zjb.pr.out
profile	/app/data/saxs_computation/zj/2zjb/2zjb.dat