SAXSdb — 4i9o

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

CREB-binding protein

Mus musculus

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 586–672	Fragment：UNP residues 562-672, GACKIX domain Mutation：L664C Non-standard monomer：Yes (specific site not provided by mmCIF)	KI1 1-{4-[4-chloro-3-(trifluoromethyl)phenyl]-4-hydroxypiperidin-1-yl}-3-sulfanylpropan-1-one × 1 EDO 1,2-ETHANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.8 M (NH4)2SO4, 0.1 M Tris-HCl, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.233
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 586–672	Fragment：UNP residues 562-672, GACKIX domain Mutation：L664C Non-standard monomer：Yes (specific site not provided by mmCIF)	KI1 1-{4-[4-chloro-3-(trifluoromethyl)phenyl]-4-hydroxypiperidin-1-yl}-3-sulfanylpropan-1-one × 2 EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.8 M (NH4)2SO4, 0.1 M Tris-HCl, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.233

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 4I9O	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1F81 SOLUTION STRUCTURE OF THE TAZ2 DOMAIN OF THE TRANSCRIPTIONAL ADAPTOR PROTEIN CBP Deposited 2000-06-28	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1764–1850（87 aa） Fragment：TAZ2 DOMAIN (1764-1850)	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 5.9；298 K；Ionic strength (raw mmCIF value) 25 mM；Pressure 1 NMR sample composition 1.5 mM Taz2 \| 25 mM deuterated acetate 0.1 mM ZnCl2 0.1 mM DTT pH 5.9	Resolution not provided
1JJS NMR Structure of IBiD, A Domain of CBP/p300 Deposited 2001-07-09	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2067–2112（46 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K	Resolution not provided
1KBH Mutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTR Deposited 2001-11-06	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 2059–2117（59 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR measurement conditions pH 6.6；31 K；Ionic strength (raw mmCIF value) 60 mM；Pressure ambient NMR sample composition 3mM U-15N,13C-CBP:2059-2117 6mM 14N,12C-ACTR:1018-1088 \| 10 mM Tris, 50 mM NaCl 95%H2O,5%D2O NMR sample composition 3mM U-15N,12C-CBP:2059-2117 6mM 14N,12C-ACTR:1018-1088 \| 10 mM Tris, 50 mM NaCl 95%H2O,5%D2O NMR sample composition 3mM U-15N,13C-CBP:2059-2117 6mM 14N,12C-ACTR:1018-1088 \| 10 mM Tris, 50 mM NaCl 100%D2O NMR sample composition 2mM U-15N,13C-ACTR:1018-1088 4mM 14N,12C-CBP:2059-2117 \| 10 mM Tris, 50 mM NaCl 95%H2O,5%D2O NMR sample composition 2mM U-15N,12C-ACTR:1018-1088 4mM 14N,12C-CBP:2059-2117 \| 10 mM Tris, 50 mM NaCl 95%H2O,5%D2O NMR sample composition 2mM U-15N,13C-ACTR:1018-1088 4mM 14N,12C-CBP:2059-2117 \| 10 mM Tris, 50 mM NaCl 100%D2O	Resolution not provided
1KDX KIX DOMAIN OF MOUSE CBP (CREB BINDING PROTEIN) IN COMPLEX WITH PHOSPHORYLATED KINASE INDUCIBLE DOMAIN (PKID) OF RAT CREB (CYCLIC AMP RESPONSE ELEMENT BINDING PROTEIN), NMR 17 STRUCTURES Deposited 1997-09-16	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 A 586–666（81 aa） Fragment：KIX, RESIDUES 586-666	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；315 K；Ionic strength (raw mmCIF value) 0.07；Pressure 1 NMR sample composition H2O OR D2O	Resolution not provided
1L8C STRUCTURAL BASIS FOR HIF-1ALPHA/CBP RECOGNITION IN THE CELLULAR HYPOXIC RESPONSE Deposited 2002-03-19	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 A 345–439（95 aa） Fragment：TAZ1 (Transcription activation zinc finger) domain, Residues 345-439	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.1；298 K；Ionic strength (raw mmCIF value) 2.0 Millimolar；Pressure Ambient NMR sample composition 1MM 13C, 15N-TAZ1, 2MM HIF-1a NMR sample composition 1MM 13C, 15N-HIF-1a, 2MM TAZ1 NMR sample composition 10MM D-TRIS, 10MM D-DTT, 0.02% NAN3, 0.5MM ZnSO4	Resolution not provided
1SB0 Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb Deposited 2004-02-09	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 A 580–666（87 aa） Fragment：KIX domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；27 K；Ionic strength (raw mmCIF value) 50 mM；Pressure ambient NMR sample composition 20 mM Tris d11 acetate d4; 50 mM NaCl; 2 mM NaN3; pH 5.5 \| 90% H20; 10% D2O	Resolution not provided
1TOT ZZ Domain of CBP- a Novel Fold for a Protein Interaction Module Deposited 2004-06-15	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1700–1751（52 aa） Fragment：ZZ domain of murine CBP (residues 1700-1751)	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 6.8；298 K；Ionic strength (raw mmCIF value) 10 mM；Pressure ambient NMR sample composition 2.3 mM solutions in degassed 10 mM Tris-d11 pH 6.8, 200 M ZnCl2, 10 mM DTT-d10, 0.05% w/v sodium azide, 94 % H2O, 6 % D2O \| 94 % H2O, 6 % D2O	Resolution not provided
1U2N Structure CBP TAZ1 Domain Deposited 2004-07-19	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 340–439（100 aa） Fragment：CBP TAZ1 Domain	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.9；298 K；Ionic strength (raw mmCIF value) 50mM；Pressure ambient NMR sample composition 1mM N15 TAZ1; 10mM Tris-d11 pH 6.9; 50mM NaCl; 2mM DTT \| 90% H2O, 10% 2H2O NMR sample composition 1mM C13,N15 TAZ1; 10mM Tris-d11 pH 6.9; 50mM NaCl; 2mM DTT \| 100% 2H2O NMR sample composition 1mM C13,N15 TAZ1; 10mM Tris-d11 pH 6.9; 50mM NaCl; 2mM DTT \| 90% H2O, 10% 2H2O	Resolution not provided
2AGH Structural basis for cooperative transcription factor binding to the CBP coactivator Deposited 2005-07-26	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 × 3 PDB declaration: trimeric	Chain B 586–672（87 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；298 K；Pressure 1 NMR sample composition 0.5-0.8 mM 15N,13C-labeled protein (e.g. CBP) + 3 fold excess of unlabeled binding partners (MYB + MLL), 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O \| 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O NMR sample composition 13C,15N-MYB + UNLABELED CBP & MYB, 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O \| 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O NMR sample composition 13C,15N-MLL + UNLABELED CBP & MLL, 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O \| 20 mM Tris-d3-acetate, 50 mM NaCl, 0.2% sodium azide, 10% D2O	Resolution not provided
2C52 Structural diversity in CBP p160 complexes Deposited 2005-10-25	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 A 2059–2117（59 aa） Fragment：SID, RESIDUES 2059-2117	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100 NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100 NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100 NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100 NMR sample composition 90% WATER/10% D2O NMR sample composition 90% WATER/10% D2O NMR sample composition 100% D2O NMR sample composition 100% D2O	Resolution not provided
2KA6 NMR structure of the CBP-TAZ2/STAT1-TAD complex Deposited 2008-10-30	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 A 1764–1855（92 aa） Fragment：UNP residues 1764 to 1855	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.8；290 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 1 mM [U-100% 15N] TAZ2, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2KKJ Solution structure of the Nuclear coactivator binding domain of CBP Deposited 2009-06-24	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2059–2117（59 aa） Fragment：Nuclear coactivator binding domain, UNP residues 2059-2441	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；31 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 10 % D2O-1, 20 mM sodium chloride-2, 20 mM sodium phosphate-3, 2 mM [U-100% 13C; U-100% 15N] protein-4, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2L14 Structure of CBP nuclear coactivator binding domain in complex with p53 TAD Deposited 2010-07-22	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 A 2059–2117（59 aa） Fragment：CBP nuclear coactivator binding domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 0.5 mM [U-99% 15N] CBP nuclear coactivator binding domain, 0.5 mM [U-99% 15N] p53 TAD, 0.5 mM [U-99% 13C; U-99% 15N] CBP nuclear coactivator binding domain, 0.5 mM [U-99% 13C; U-99% 15N] p53 TAD, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2LQH NMR structure of FOXO3a transactivation domains (CR2C-CR3) in complex with CBP KIX domain (2b3l conformation) Deposited 2012-03-06	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 A 586–672（87 aa） Fragment：KIX domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] KIX, 0.6 mM CR2C-CR3, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] KIX, 0.6 mM CR2C-CR3, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 100% D2O \| 100% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] CR2C-CR3, 0.6 mM KIX, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] CR2C-CR3, 0.6 mM KIX, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 100% D2O \| 100% D2O	Resolution not provided
2LQI NMR structure of FOXO3a transactivation domains (CR2C-CR3) in complex with CBP KIX domain (2l3b conformation) Deposited 2012-03-06	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 A 586–672（87 aa） Fragment：KIX DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] KIX, 0.6 mM CR2C-CR3, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] KIX, 0.6 mM CR2C-CR3, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 100% D2O \| 100% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] CR2C-CR3, 0.6 mM KIX, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] CR2C-CR3, 0.6 mM KIX, 20 mM MES, 50 mM sodium chloride, 1 mM DTT, 100% D2O \| 100% D2O	Resolution not provided
2LWW NMR structure of RelA-TAD/CBP-TAZ1 complex Deposited 2012-08-07	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 A 340–439（100 aa） Fragment：TAZ-type 1 zinc finger residues 340-439	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 40；Pressure ambient NMR sample composition 0.8-1.1 mM [U-13C; U-15N] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.8-1.1 mM [U-13C] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM [U-2H] DTT, 20 mM [U-2H] TRIS, 40 mM sodium chloride, 99.8 % [U-2H] D2O, 100% D2O \| 100% D2O NMR sample composition 0.7-0.9 mM [U-13C] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM [U-2H] DTT, 20 mM [U-2H] TRIS, 40 mM sodium chloride, 99.8 % [U-2H] D2O, 100% D2O \| 100% D2O NMR sample composition 0.7-0.9 mM [U-13C; U-15N] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.8-1.1 mM [U-15N] TAZ1, 1.2-1.5 mM RelA-TA2, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.7-0.9 mM [U-15N] RelA-TA2, 1.5-1.8 mM TAZ1, 2 mM DTT, 20 mM TRIS, 40 mM sodium chloride, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
5HOU Solution Structure of p53TAD-TAZ1 Deposited 2016-01-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 340–439（100 aa） Fragment：p53TAD, TAZ1 domain of CBP	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.8；308 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR measurement conditions pH 6.4；308 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 1.0 mM [U-15N] p53TAD - [NA] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O, 5% D2O \| 95% H2O/5% D2O NMR sample composition 1.0 mM [U-15N][U-13C] p53TAD - [NA] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1.0 mM [NA] p53TAD - [U-15N] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1.0 mM [NA] p53TAD - [U-15N][U-13C] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1.0 mM [U-15N][U-13C] p53TAD - [NA] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1 mM [NA] p53TAD - [U-15N][U-13C] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
5HP0 Solution Structure of TAZ2-p53AD2 Deposited 2016-01-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1764–1855（92 aa） Fragment：p53AD2, TAZ2 domain of CBP	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.8；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR measurement conditions pH 6.4；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 1 mM [U-13C; U-15N] TAZ2-p53AD2, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-13C; U-15N] TAZ2-p53AD2, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM [U-13C; U-15N] TAZ2-p53AD2, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-13C] TAZ2, 1 mM p53AD2(38-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 5 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM [U-13C] p53AD2, 1 mM TAZ2, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O	Resolution not provided
5HPD Solution Structure of TAZ2-p53TAD Deposited 2016-01-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1764–1855（92 aa） Fragment：p53TAD, TAZ2 domain of CBP	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.8；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR measurement conditions pH 6.4；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 1.75 mM [U-13C; U-15N] TAZ2-p53TAD, 20 mM TRIS, 50 mM sodium chloride, 1 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.75 mM [U-13C; U-15N] TAZ2-p53TAD, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 1 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM [U-13C] TAZ2, 1 mM p53(13-37, 1 mM p53(38-61), 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 20 mM [U-2H] TRIS, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM TAZ2, 1 mM [U-13C] p53(13-37), 1 mM [U-13C] p53(38-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM TAZ2, 1 mM [U-15N] p53(13-61), 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-15N] TAZ2, 1 mM p53(13-61), 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM TAZ2, 1 mM [U-13C] p53(13-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O NMR sample composition 1 mM [U-13C] TAZ2, 1 mM p53(13-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O \| 99% D2O, 1% H2O	Resolution not provided
5W0I CREBBP Bromodomain in complex with Cpd8 (1-(3-(7-(difluoromethyl)-6-(1-methyl-1H-pyrazol-4-yl)-3,4-dihydroquinolin-1(2H)-yl)-1-(tetrahydrofuran-3-yl)-1,4,6,7-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl)ethan-1-one) Deposited 2017-05-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1083–1198（116 aa） Fragment：Bromodomain, UNP residues 1083-1198	Not recorded	9UA 1-{3-[7-(difluoromethyl)-6-(1-methyl-1H-pyrazol-4-yl)-3,4-dihydroquinolin-1(2H)-yl]-1-[(3S)-oxolan-3-yl]-1,4,6,7-tetrahydro-5H-pyrazolo[4,3-c]pyridin-5-yl}ethan-1-one × 1 DMS DIMETHYL SULFOXIDE × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；277 K；0.2 M Li2SO4, 0.1M Bis-Tris pH 6.5, 23% PEG33500	Resolution 1.43 Å R-free 0.192
6DMX HBZ56 in complex with KIX and c-Myb Deposited 2018-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 586–672（87 aa） Fragment：residues 284-315 Chain D 586–672（87 aa） Fragment：residues 284-315	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, ammonium iodide	Resolution 2.80 Å R-free 0.301
6DMX HBZ56 in complex with KIX and c-Myb Deposited 2018-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain G 586–672（87 aa） Fragment：residues 284-315 Chain I 586–672（87 aa） Fragment：residues 284-315	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, ammonium iodide	Resolution 2.80 Å R-free 0.301
6DNQ HBZ77 in complex with KIX and c-Myb Deposited 2018-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 586–672（87 aa） Fragment：residues 586-672 Chain D 586–672（87 aa） Fragment：residues 586-672	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG 3350, calcium chloride	Resolution 2.35 Å R-free 0.229
7LVS The CBP TAZ1 Domain in Complex with a CITED2-HIF-1-Alpha Fusion Peptide Deposited 2021-02-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 340–439（100 aa）	Not recorded	ZN ZINC ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M HEPES pH 6.87, 28% PEG 4000	Resolution 2.02 Å R-free 0.241

23 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CBP_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 15–101； UniProt 586–672

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	4i9o
Deposition date deposition_date	2012-12-05
Structure title title	Crystal Structure of GACKIX L664C Tethered to 1-10
Keywords keywords	KIX domain, Transcriptional Coactivator, TRANSFERASE; TRANSFERASE
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	14.52 Å
Radius of gyration Rg (electron density) rg_electron	13.32 Å
Forward intensity I(0) i0	1983280.00
Molecular weight molecular_weight	9459.0 kDa
Excluded volume excluded_volume	11704 Å³
Envelope volume envelope_volume	13701 Å³
Hydration-shell volume shell_volume	9326 Å³
Envelope diameter envelope_diameter	46.7 Å
Shell Rg shell_rg	18.05 Å
Envelope Rg envelope_rg	13.72 Å
Shape Rg shape_rg	13.34 Å
Total Rg total_rg	14.33 Å
Total atoms total_atoms	657
Residues n_residues	76
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	48.8 Å
Rg (real space) rg_real	14.54 Å
Rg uncertainty (real space) rg_real_error	0.29 Å
I(0) (real space) i0_real	1.9830e+06
I(0) uncertainty (real space) i0_real_error	1.9480e+04
Rg (reciprocal space) rg_reciprocal	14.54 Å
I(0) (reciprocal space) i0_reciprocal	1983000.0000
Solution quality estimate total_estimate	0.8786
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	16.1 Å
Skewness Skewness skewness	0.369
Kurtosis Kurtosis kurtosis	-0.282
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	320800.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.819; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 1.000

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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	CREB-binding protein
Molecular weight formula_weight	12139.2 kDa
EC 编号 ec_number	2.3.1.48
Mutation mutation	L664C
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	694

MRGSHHHHHHGMASGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKECEEKRRSRL

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	1-{4-[4-chloro-3-(trifluoromethyl)phenyl]-4-hydroxypiperidin-1-yl}-3-sulfanylpropan-1-one
Molecular weight formula_weight	367.8 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 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	27

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d4i9oa_
Class class	a — All alpha proteins
Fold Fold fold	a.12 — Kix domain of CBP (creb binding protein)
Superfamily Superfamily superfamily	a.12.1 — Kix domain of CBP (creb binding protein)
Family Family family	a.12.1.1 — Kix domain of CBP (creb binding protein)

CATH v4.4 (1 domains)

Domain ID domain_id	4i9oA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily	20 — Coactivator CBP, KIX domain

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8. Citations (1)

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Unit-cell length a length_a	48.330 Å
Unit-cell length b length_b	48.330 Å
Unit-cell length c length_c	85.464 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	8

Space group space_group	P 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	42.070 Å
R factor r_factor	0.2076
R_work r_work	0.2064
R_free r_free	0.2329

fit	/app/data/saxs_computation/i9/4i9o/4i9o.fit
pddf	/app/data/pr_computation/i9/4i9o/4i9o.pr.out
profile	/app/data/saxs_computation/i9/4i9o/4i9o.dat

Crystal Structure of GACKIX L664C Tethered to 1-10

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

CREB-binding 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

Diffraction experiment Diffraction