SAXSdb — 5tuv

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

Transcription factor DP1

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 199–350	Fragment：UNP residues 199-350	Transcription factor E2F5 × 1 （Q15329） Retinoblastoma-like protein 1 × 1 （P28749）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；100mM Hepes pH 7.0, 7% PEG 5000, 5% 1-propanol, 2% 2-propanol	Resolution 2.90 Å R-free 0.260
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 199–350	Fragment：UNP residues 199-350	Transcription factor E2F5 × 1 （Q15329） Retinoblastoma-like protein 1 × 1 （P28749）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；100mM Hepes pH 7.0, 7% PEG 5000, 5% 1-propanol, 2% 2-propanol	Resolution 2.90 Å R-free 0.260
3	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 199–350 Chain D； UniProt 199–350	Fragment：UNP residues 199-350	Transcription factor E2F5 × 2 （Q15329） Retinoblastoma-like protein 1 × 2 （P28749）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；100mM Hepes pH 7.0, 7% PEG 5000, 5% 1-propanol, 2% 2-propanol	Resolution 2.90 Å R-free 0.260

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 5TUV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2AZE Structure of the Rb C-terminal domain bound to an E2F1-DP1 heterodimer Deposited 2005-09-10	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 199–350（152 aa） Fragment：coiled coil and marked box domains (residues 199-350)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；Sodium Citrate, Ammonium Sulfate, PEG 400, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.55 Å R-free 0.262
2AZE Structure of the Rb C-terminal domain bound to an E2F1-DP1 heterodimer Deposited 2005-09-10	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 199–350（152 aa） Fragment：coiled coil and marked box domains (residues 199-350)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；Sodium Citrate, Ammonium Sulfate, PEG 400, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.55 Å R-free 0.262
5TUU Crystal structure of the E2F4-DP1 coiled coil and marked-box domains Deposited 2016-11-07	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 199–350（152 aa） Fragment：UNP residues 199-350	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1M MES pH 6.5, 15% PEG 6000	Resolution 2.25 Å R-free 0.239
5TUU Crystal structure of the E2F4-DP1 coiled coil and marked-box domains Deposited 2016-11-07	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 199–350（152 aa） Fragment：UNP residues 199-350	Not recorded	GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1M MES pH 6.5, 15% PEG 6000	Resolution 2.25 Å R-free 0.239

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TFDP1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–155； UniProt 199–350 Author chain D； PDBConstruct 4–155； UniProt 199–350

Transcription factor E2F5

Homo sapiens

UniProt Q15329

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 124–232	Fragment：UNP residues 124-232	Transcription factor DP1 × 1 （Q14186） Retinoblastoma-like protein 1 × 1 （P28749）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；100mM Hepes pH 7.0, 7% PEG 5000, 5% 1-propanol, 2% 2-propanol	Resolution 2.90 Å R-free 0.260
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain E； UniProt 124–232	Fragment：UNP residues 124-232	Transcription factor DP1 × 1 （Q14186） Retinoblastoma-like protein 1 × 1 （P28749）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；100mM Hepes pH 7.0, 7% PEG 5000, 5% 1-propanol, 2% 2-propanol	Resolution 2.90 Å R-free 0.260
3	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain B； UniProt 124–232 Chain E； UniProt 124–232	Fragment：UNP residues 124-232	Transcription factor DP1 × 2 （Q14186） Retinoblastoma-like protein 1 × 2 （P28749）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；100mM Hepes pH 7.0, 7% PEG 5000, 5% 1-propanol, 2% 2-propanol	Resolution 2.90 Å R-free 0.260

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	E2F5_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 4–112； UniProt 124–232 Author chain E； PDBConstruct 4–112； UniProt 124–232

Retinoblastoma-like protein 1

Homo sapiens

UniProt P28749

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain C； UniProt 994–1031	Fragment：UNP residues 994-1031	Transcription factor DP1 × 1 （Q14186） Transcription factor E2F5 × 1 （Q15329）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；100mM Hepes pH 7.0, 7% PEG 5000, 5% 1-propanol, 2% 2-propanol	Resolution 2.90 Å R-free 0.260
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain F； UniProt 994–1031	Fragment：UNP residues 994-1031	Transcription factor DP1 × 1 （Q14186） Transcription factor E2F5 × 1 （Q15329）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；100mM Hepes pH 7.0, 7% PEG 5000, 5% 1-propanol, 2% 2-propanol	Resolution 2.90 Å R-free 0.260
3	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain C； UniProt 994–1031 Chain F； UniProt 994–1031	Fragment：UNP residues 994-1031	Transcription factor DP1 × 2 （Q14186） Transcription factor E2F5 × 2 （Q15329）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；295 K；100mM Hepes pH 7.0, 7% PEG 5000, 5% 1-propanol, 2% 2-propanol	Resolution 2.90 Å R-free 0.260

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 5TUV	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1H28 CDK2/CyclinA in complex with an 11-residue recruitment peptide from p107 Deposited 2002-07-31	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 653–663（11 aa） Fragment：RB PEPTIDE, RESIDUES 653-663	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.8M KCL, 1.2M (NH4)2SO4, 40MM HEPES PH 7.0. PROTEIN CONCENTRATION = 10MG/ML	Resolution 2.80 Å R-free 0.323
1H28 CDK2/CyclinA in complex with an 11-residue recruitment peptide from p107 Deposited 2002-07-31	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 653–663（11 aa） Fragment：RB PEPTIDE, RESIDUES 653-663	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；0.8M KCL, 1.2M (NH4)2SO4, 40MM HEPES PH 7.0. PROTEIN CONCENTRATION = 10MG/ML	Resolution 2.80 Å R-free 0.323
4YOO p107 pocket domain in complex with LIN52 P29A peptide Deposited 2015-03-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 391–600（210 aa） Fragment：unp residues 391-600,unp residues 781-972 Chain A 781–972（192 aa） Fragment：unp residues 391-600,unp residues 781-972	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；MES, PEG 400 4%, 1.6M ammonium sulfate	Resolution 2.40 Å R-free 0.242
4YOS p107 pocket domain complexed with LIN52 peptide Deposited 2015-03-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 391–600（210 aa） Fragment：unp residues 391-600,unp residues 781-969,unp residues 391-600,unp residues 781-969	Not recorded	SO4 SULFATE ION × 2 EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；MES, PEG 400 4%, 1.6M ammonium sulfate	Resolution 2.30 Å R-free 0.242
4YOZ p107 pocket domain in complex with HPV E7 peptide Deposited 2015-03-12	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 391–593（203 aa） Fragment：unp residues 391-593,unp residues 391-593 Chain A 777–972（196 aa） Fragment：unp residues 391-593,unp residues 391-593	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；Hepes, Ammonium Sulfate, PEG 400	Resolution 2.25 Å R-free 0.240
7SMC p107 pocket domain complexed with ARID4A peptide Deposited 2021-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 391–601（211 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain A 780–887（108 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain A 924–972（49 aa） Fragment：UNP residues 391-601,780-887,924-972	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate	Resolution 2.70 Å R-free 0.298
7SMC p107 pocket domain complexed with ARID4A peptide Deposited 2021-10-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 391–601（211 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain C 780–887（108 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain C 924–972（49 aa） Fragment：UNP residues 391-601,780-887,924-972	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate	Resolution 2.70 Å R-free 0.298
7SMD p107 pocket domain complexed with EID1 peptide Deposited 2021-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 391–601（211 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain A 780–887（108 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain A 924–972（49 aa） Fragment：UNP residues 391-601,780-887,924-972	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate	Resolution 2.15 Å R-free 0.259
7SME p107 pocket domain complexed with HDAC1 peptide Deposited 2021-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 391–601（211 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain A 780–887（108 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain A 924–972（49 aa） Fragment：UNP residues 391-601,780-887,924-972	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate	Resolution 2.64 Å R-free 0.277
7SMF p107 pocket domain complexed with mutated HDAC1-3X peptide Deposited 2021-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 391–601（211 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain A 780–887（108 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain A 924–972（49 aa） Fragment：UNP residues 391-601,780-887,924-972	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate	Resolution 3.00 Å R-free 0.301
7SMF p107 pocket domain complexed with mutated HDAC1-3X peptide Deposited 2021-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 391–601（211 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain C 780–887（108 aa） Fragment：UNP residues 391-601,780-887,924-972 Chain C 924–972（49 aa） Fragment：UNP residues 391-601,780-887,924-972	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate	Resolution 3.00 Å R-free 0.301
9C6B PP2A:B55-p107 substrate complex Deposited 2024-06-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 612–687（76 aa） Fragment：residues 612-687	Not recorded	FE2 FE (II) ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å

9 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RBL1_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 4–41； UniProt 994–1031 Author chain F； PDBConstruct 4–41； UniProt 994–1031

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	5tuv
Deposition date deposition_date	2016-11-07
Structure title title	Crystal structure of the E2F5-DP1-p107 ternary complex
Keywords keywords	Transcription factor, cell-cycle regulation, TRANSCRIPTION; TRANSCRIPTION
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	30.38 Å
Radius of gyration Rg (electron density) rg_electron	30.26 Å
Forward intensity I(0) i0	43387400.00
Molecular weight molecular_weight	50147.0 kDa
Excluded volume excluded_volume	62388 Å³
Envelope volume envelope_volume	88650 Å³
Hydration-shell volume shell_volume	27437 Å³
Envelope diameter envelope_diameter	139.7 Å
Shell Rg shell_rg	32.96 Å
Envelope Rg envelope_rg	31.80 Å
Shape Rg shape_rg	30.25 Å
Total Rg total_rg	30.55 Å
Total atoms total_atoms	3532
Residues n_residues	462
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	81.9 Å
Rg (real space) rg_real	28.22 Å
Rg uncertainty (real space) rg_real_error	0.20 Å
I(0) (real space) i0_real	4.1270e+07
I(0) uncertainty (real space) i0_real_error	4.4910e+05
Rg (reciprocal space) rg_reciprocal	30.67 Å
I(0) (reciprocal space) i0_reciprocal	43380000.0000
Solution quality estimate total_estimate	0.6805
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	31.5 Å
Skewness Skewness skewness	0.423
Kurtosis Kurtosis kurtosis	-0.414
Angular range angular_range	— – 0.2600 Å⁻¹
Current regularization parameter α current_alpha	1.7550
Highest regularization parameter α highest_alpha	3598000.0000
Real-space data points n_real_points	53
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.002; Oscil: 0.973; Stabil: 0.981; Sysdev: 0.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Transcription factor DP1
Molecular weight formula_weight	17603.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D
Atom count atom_count	3532

GEFAQECQNLEVERQRRLERIKQKQSQLQELILQQIAFKNLVQRNRHAEQQASRPPPPNSVIHLPFIIVNTSKKTVIDCSISNDKFEYLFNFDNTFEIHDDIEVLKRMGMACGLESGSCSAEDLKMARSLVPKALEPYVTEMAQGTVGGVFITTA

来源 Source

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 BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Transcription factor E2F5
Molecular weight formula_weight	12962.7 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,E

GHMKEVIDRLRYLKAEIEDLELKERELDQQKLWLQQSIKNVMDDSINNRFSYVTHEDICNCFNGDTLLAIQAPSGTQLEVPIPEMGQNGQKKYQINLKSHSGPIHVLLINKE

来源 Source

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 BL21(DE3)

Entity 3 Entity 3 polymer

Description description	Retinoblastoma-like protein 1
Molecular weight formula_weight	4663.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,F

GEFSGLTPRSALLYKFNGSPSKSLKDINNMIRQGEQRTKKR

来源 Source

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 BL21(DE3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d5tuvb_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.63 — E2F-DP heterodimerization region
Superfamily Superfamily superfamily	e.63.1 — E2F-DP heterodimerization region
Family Family family	e.63.1.0 — automated matches

Domain ID domain_id	d5tuve_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.63 — E2F-DP heterodimerization region
Superfamily Superfamily superfamily	e.63.1 — E2F-DP heterodimerization region
Family Family family	e.63.1.0 — automated matches

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8. Citations (1)

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Unit-cell length a length_a	60.980 Å
Unit-cell length b length_b	57.340 Å
Unit-cell length c length_c	99.198 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	96.64 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	49.266 Å
R factor r_factor	0.2147
R_work r_work	0.2122
R_free r_free	0.2601

fit	/app/data/saxs_computation/tu/5tuv/5tuv.fit
pddf	/app/data/pr_computation/tu/5tuv/5tuv.pr.out
profile	/app/data/saxs_computation/tu/5tuv/5tuv.dat

Crystal structure of the E2F5-DP1-p107 ternary complex

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

Transcription factor DP1

State in the Current Structure

Other States of the Same Protein in the Database

Transcription factor E2F5

State in the Current Structure

Other States of the Same Protein in the Database

Retinoblastoma-like protein 1

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)