SAXSdb — 2r7g

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

Retinoblastoma-associated protein

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 × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain A； UniProt 380–581 Chain A； UniProt 643–787 Chain C； UniProt 380–581 Chain C； UniProt 643–787	Fragment：Pocket domain, deletion of residues 582-642	Early E1A 32 kDa protein × 3 （P03255） SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 6；293 K；15mM magnesium acetate tetrahydrate, 50mM sodium cacodylate trihydrate, pH 6.0 and 1.7M ammonium sulfate, VAPOR DIFFUSION, temperature 293K	Resolution 1.67 Å R-free 0.218

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 2R7G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AD6 DOMAIN A OF HUMAN RETINOBLASTOMA TUMOR SUPPRESSOR Deposited 1997-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 378–562（185 aa） Fragment：DOMAIN A	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6.0	Resolution 2.30 Å R-free 0.240
1GH6 RETINOBLASTOMA POCKET COMPLEXED WITH SV40 LARGE T ANTIGEN Deposited 2000-11-15	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 B 379–577（199 aa） Fragment：UNP residues 379-577 and 645-772 Chain B 645–772（128 aa） Fragment：UNP residues 379-577 and 645-772	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.2；pH 7.2	Resolution 3.20 Å R-free 0.314
1GUX RB POCKET BOUND TO E7 LXCXE MOTIF Deposited 1997-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 372–589（218 aa） Fragment：POCKET DOMAIN Chain B 636–787（152 aa） Fragment：POCKET DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；3.5 M SODIUM FORMATE, 0.1M NA HEPES PH 7.5, 20 MIROMOLAR CDCL2	Resolution 1.85 Å R-free 0.289
1H25 CDK2/Cyclin A in complex with an 11-residue recruitment peptide from retinoblastoma-associated protein Deposited 2002-07-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 868–878（11 aa） Fragment：RESIDUES 869-878	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 2.50 Å R-free 0.266
1O9K Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F peptide Deposited 2002-12-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 372–589（218 aa） Fragment：DOMAIN A, RESIDUES 372-589 Chain B 636–787（152 aa） Fragment：DOMAIN B, RESIDUES 636-787	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；pH 7.80	Resolution 2.60 Å R-free 0.285
1O9K Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F peptide Deposited 2002-12-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 372–589（218 aa） Fragment：DOMAIN A, RESIDUES 372-589 Chain D 636–787（152 aa） Fragment：DOMAIN B, RESIDUES 636-787	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；pH 7.80	Resolution 2.60 Å R-free 0.285
1O9K Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F peptide Deposited 2002-12-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 372–589（218 aa） Fragment：DOMAIN A, RESIDUES 372-589 Chain F 636–787（152 aa） Fragment：DOMAIN B, RESIDUES 636-787	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；pH 7.80	Resolution 2.60 Å R-free 0.285
1O9K Crystal structure of the retinoblastoma tumour suppressor protein bound to E2F peptide Deposited 2002-12-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 372–589（218 aa） Fragment：DOMAIN A, RESIDUES 372-589 Chain H 636–787（152 aa） Fragment：DOMAIN B, RESIDUES 636-787	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；pH 7.80	Resolution 2.60 Å R-free 0.285
1PJM Mouse Importin alpha-bipartite NLS from human retinoblastoma protein Complex Deposited 2003-06-03	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 857–876（20 aa） Fragment：NLS (nuclear localization signal) bipartite peptide	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；Sodium Citrate, DTT, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.50 Å R-free 0.239
2AZE Structure of the Rb C-terminal domain bound to an E2F1-DP1 heterodimer Deposited 2005-09-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 829–874（46 aa） Fragment：C-terminal core domain (residues 829-874)	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 mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 829–874（46 aa） Fragment：C-terminal core domain (residues 829-874)	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
2QDJ Crystal structure of the Retinoblastoma protein N-domain provides insight into tumor suppression, ligand interaction and holoprotein architecture Deposited 2007-06-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 52–355（304 aa） Fragment：N-terminal domain	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；0.2 M Na acetate, 25% (w/v) PEG 4000, 0.1 M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.276
3N5U Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1 Deposited 2010-05-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 870–882（13 aa） Fragment：UNP residues 870-882	Not recorded	MN MANGANESE (II) ION × 4 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions hanging drop；pH 7.5；298 K；100mM HEPES, 200mM MgCl2, 18% PEG 4000, pH 7.5, hanging drop, temperature 298K	Resolution 3.20 Å R-free 0.261
3N5U Crystal structure of an Rb C-terminal peptide bound to the catalytic subunit of PP1 Deposited 2010-05-25	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 870–882（13 aa） Fragment：UNP residues 870-882	Not recorded	MN MANGANESE (II) ION × 2 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions hanging drop；pH 7.5；298 K；100mM HEPES, 200mM MgCl2, 18% PEG 4000, pH 7.5, hanging drop, temperature 298K	Resolution 3.20 Å R-free 0.261
3POM Crystal Structure of the Unliganded Retinoblastoma Protein Pocket Domain Deposited 2010-11-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 380–577（198 aa） Fragment：Pocket Domain, Domain A, UNP residues 380-577, Domain B, UNP residues 643-787 Chain A 643–783（141 aa） Fragment：Pocket Domain, Domain A, UNP residues 380-577, Domain B, UNP residues 643-787	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 10.6；277 K；100 mM CAPS, 10% PEG 3350, pH 10.6, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.50 Å R-free 0.262
3POM Crystal Structure of the Unliganded Retinoblastoma Protein Pocket Domain Deposited 2010-11-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 380–577（198 aa） Fragment：Pocket Domain, Domain A, UNP residues 380-577, Domain B, UNP residues 643-787 Chain B 643–783（141 aa） Fragment：Pocket Domain, Domain A, UNP residues 380-577, Domain B, UNP residues 643-787	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 10.6；277 K；100 mM CAPS, 10% PEG 3350, pH 10.6, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.50 Å R-free 0.262
4ELJ Crystal structure of the inactive retinoblastoma protein phosphorylated at T373 Deposited 2012-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 53–244（192 aa） Fragment：UNP residues 53-244, 268-582, 642-787 Chain A 268–582（315 aa） Fragment：UNP residues 53-244, 268-582, 642-787 Chain A 642–787（146 aa） Fragment：UNP residues 53-244, 268-582, 642-787	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277.15 K；100mM HEPES, 100mM Ammonium Fluoride, 16% PEG4K, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 2.70 Å R-free 0.266
4ELL Structure of the inactive retinoblastoma protein pocket domain Deposited 2012-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 380–787（408 aa） Fragment：POCKET DOMAIN, UNP residues 380-787	Mutation：S608E, L561F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277.15 K；100mM sodium citrate, 1mM LiCl, 18% PEG 8K., pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 1.98 Å R-free 0.238
4ELL Structure of the inactive retinoblastoma protein pocket domain Deposited 2012-04-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 380–787（408 aa） Fragment：POCKET DOMAIN, UNP residues 380-787	Mutation：S608E, L561F	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277.15 K；100mM sodium citrate, 1mM LiCl, 18% PEG 8K., pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K	Resolution 1.98 Å R-free 0.238
9DGK The Retinoblastoma Protein with Mutation M704V Deposited 2024-09-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 380–793（414 aa）	Mutation：M704V, S608E, S612A, S780A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；18% PEG 8K, 0.1M sodium citrate, 0.1M succinate pH 5.5, 1M lithium chloride	Resolution 2.38 Å R-free 0.277
9DGK The Retinoblastoma Protein with Mutation M704V Deposited 2024-09-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 380–793（414 aa）	Mutation：M704V, S608E, S612A, S780A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；18% PEG 8K, 0.1M sodium citrate, 0.1M succinate pH 5.5, 1M lithium chloride	Resolution 2.38 Å R-free 0.277
9DHC The Retinoblastoma Protein with Mutation S751Y Deposited 2024-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 380–793（414 aa）	Mutation：S751Y, S608E, S612A, S780A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；18% PEG 8K, 0.1M sodium citrate, 0.1M succinate pH5.5, 1M lithium chloride	Resolution 2.32 Å R-free 0.263
9DHC The Retinoblastoma Protein with Mutation S751Y Deposited 2024-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 380–793（414 aa）	Mutation：S751Y, S608E, S612A, S780A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；18% PEG 8K, 0.1M sodium citrate, 0.1M succinate pH5.5, 1M lithium chloride	Resolution 2.32 Å R-free 0.263
9DHF The Retinoblastoma Protein with Mutation E554K Deposited 2024-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 380–793（414 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；18% PEG8K, 0.1M sodium citrate, 0.1M succinate pH 5.5, 1M lithium chloride	Resolution 2.26 Å R-free 0.265
9DHF The Retinoblastoma Protein with Mutation E554K Deposited 2024-09-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 380–793（414 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；18% PEG8K, 0.1M sodium citrate, 0.1M succinate pH 5.5, 1M lithium chloride	Resolution 2.26 Å R-free 0.265
9DHU The Retinoblastoma Protein with Mutation E533K Deposited 2024-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 380–786（407 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277.15 K；PEG 8K (18%), 0.1M sodium citrate, 0.1M succinate pH 5.5, 1M lithium chloride	Resolution 2.16 Å R-free 0.263
9DHU The Retinoblastoma Protein with Mutation E533K Deposited 2024-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 380–786（407 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277.15 K；PEG 8K (18%), 0.1M sodium citrate, 0.1M succinate pH 5.5, 1M lithium chloride	Resolution 2.16 Å R-free 0.263

16 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RB_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–202； UniProt 380–581 Author chain A； PDBConstruct 203–347； UniProt 643–787 Author chain C； PDBConstruct 1–202； UniProt 380–581 Author chain C； PDBConstruct 203–347； UniProt 643–787

Early E1A 32 kDa protein

Human adenovirus 5

UniProt P03255

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 × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain B； UniProt 40–49 Chain D； UniProt 40–49 Chain E； UniProt 40–49	Fragment：CR1 domain	Retinoblastoma-associated protein × 2 （P06400） SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 6；293 K；15mM magnesium acetate tetrahydrate, 50mM sodium cacodylate trihydrate, pH 6.0 and 1.7M ammonium sulfate, VAPOR DIFFUSION, temperature 293K	Resolution 1.67 Å R-free 0.218

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 2R7G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2KJE NMR structure of CBP TAZ2 and adenoviral E1A complex Deposited 2009-05-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 53–91（39 aa） Fragment：UNP residues 53-91	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.8；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 1-1.5 mM [U-100% 13C; U-100% 15N] TRIS-1, 1-1.5 mM [U-100% 15N] TRIS-2, 100% D2O \| 100% D2O	Resolution not provided
6H6D Crystal structures of the murine class I major histocompatibility complex H-2Db in complex with adenovirus-derived peptide Ad10 Deposited 2018-07-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 234–243（10 aa）	Not recorded	SO4 SULFATE ION × 3 GOL GLYCEROL × 5 CL CHLORIDE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；277 K；1.8M ammonium sulphate, 0.1M Tris	Resolution 2.40 Å R-free 0.233
6H6D Crystal structures of the murine class I major histocompatibility complex H-2Db in complex with adenovirus-derived peptide Ad10 Deposited 2018-07-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 234–243（10 aa）	Not recorded	SO4 SULFATE ION × 1 GOL GLYCEROL × 3 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；277 K；1.8M ammonium sulphate, 0.1M Tris	Resolution 2.40 Å R-free 0.233

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	E1A_ADE05
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–10； UniProt 40–49 Author chain D； PDBConstruct 1–10； UniProt 40–49 Author chain E； PDBConstruct 1–10； UniProt 40–49

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	2r7g
Deposition date deposition_date	2007-09-07
Structure title title	Structure of the retinoblastoma protein pocket domain in complex with adenovirus E1A CR1 domain
Keywords keywords	Retinoblastoma protein, E1A, E2F displacement, TRANSCRIPTION REPRESSOR, CELL CYCLE; TRANSCRIPTION REPRESSOR, CELL CYCLE
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	30.48 Å
Radius of gyration Rg (electron density) rg_electron	29.97 Å
Forward intensity I(0) i0	100320000.00
Molecular weight molecular_weight	82383.0 kDa
Excluded volume excluded_volume	104490 Å³
Envelope volume envelope_volume	130030 Å³
Hydration-shell volume shell_volume	37056 Å³
Envelope diameter envelope_diameter	109.4 Å
Shell Rg shell_rg	36.37 Å
Envelope Rg envelope_rg	30.13 Å
Shape Rg shape_rg	29.94 Å
Total Rg total_rg	30.66 Å
Total atoms total_atoms	5785
Residues n_residues	702
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	103.6 Å
Rg (real space) rg_real	30.53 Å
Rg uncertainty (real space) rg_real_error	0.86 Å
I(0) (real space) i0_real	1.0030e+08
I(0) uncertainty (real space) i0_real_error	1.6900e+06
Rg (reciprocal space) rg_reciprocal	30.51 Å
I(0) (reciprocal space) i0_reciprocal	100300000.0000
Solution quality estimate total_estimate	0.8729
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	35.9 Å
Skewness Skewness skewness	0.419
Kurtosis Kurtosis kurtosis	-0.202
Angular range angular_range	— – 0.2600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	47720000.0000
Real-space data points n_real_points	53
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.821; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.918

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Retinoblastoma-associated protein
Molecular weight formula_weight	40728.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	6267

NTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPR

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	Early E1A 32 kDa protein
Molecular weight formula_weight	1198.3 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

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

PPTLHELYDL

来源 Source

来源生物 organism	Human adenovirus 5
NCBI Class编号 ncbi_taxonomy_id	28285
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	482

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2r7ga1
Class class	a — All alpha proteins
Fold Fold fold	a.74 — Cyclin-like
Superfamily Superfamily superfamily	a.74.1 — Cyclin-like
Family Family family	a.74.1.3 — Retinoblastoma tumor suppressor domains

Domain ID domain_id	d2r7ga2
Class class	a — All alpha proteins
Fold Fold fold	a.74 — Cyclin-like
Superfamily Superfamily superfamily	a.74.1 — Cyclin-like
Family Family family	a.74.1.3 — Retinoblastoma tumor suppressor domains

Domain ID domain_id	d2r7gc1
Class class	a — All alpha proteins
Fold Fold fold	a.74 — Cyclin-like
Superfamily Superfamily superfamily	a.74.1 — Cyclin-like
Family Family family	a.74.1.3 — Retinoblastoma tumor suppressor domains

Domain ID domain_id	d2r7gc2
Class class	a — All alpha proteins
Fold Fold fold	a.74 — Cyclin-like
Superfamily Superfamily superfamily	a.74.1 — Cyclin-like
Family Family family	a.74.1.3 — Retinoblastoma tumor suppressor domains

CATH v4.4 (4 domains)

Domain ID domain_id	2r7gA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	472 — Cyclin A; domain 1
Homologous superfamily homologous superfamily	10 — Cyclin-like

Domain ID domain_id	2r7gA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	472 — Cyclin A; domain 1
Homologous superfamily homologous superfamily	10 — Cyclin-like

Domain ID domain_id	2r7gC01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	472 — Cyclin A; domain 1
Homologous superfamily homologous superfamily	10 — Cyclin-like

Domain ID domain_id	2r7gC02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	472 — Cyclin A; domain 1
Homologous superfamily homologous superfamily	10 — Cyclin-like

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8. Citations (1)

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Unit-cell length a length_a	57.713 Å
Unit-cell length b length_b	57.706 Å
Unit-cell length c length_c	92.268 Å
Unit-cell angle α angle_alpha	94.34 °
Unit-cell angle β angle_beta	92.69 °
Unit-cell angle γ angle_gamma	105.79 °
Molecules per unit cell Z z_pdb	3

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

Resolution resolution	1.671 Å
Low-resolution limit resolution_low	40.820 Å
R factor r_factor	0.1976
R_work r_work	0.1953
R_free r_free	0.2182

fit	/app/data/saxs_computation/r7/2r7g/2r7g.fit
pddf	/app/data/pr_computation/r7/2r7g/2r7g.pr.out
profile	/app/data/saxs_computation/r7/2r7g/2r7g.dat

Structure of the retinoblastoma protein pocket domain in complex with adenovirus E1A CR1 domain

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

Retinoblastoma-associated protein

State in the Current Structure

Other States of the Same Protein in the Database

Early E1A 32 kDa protein

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

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)