SAXSdb — 2col

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

Bifunctional hemolysin-adenylate cyclase

Bordetella pertussis

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 7–362	Not recorded	Calmodulin × 1 （P62155） MG MAGNESIUM ION × 2 POP PYROPHOSPHATE 2- × 1 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.6；278 K；PEG4000, Na Citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 2.20 Å R-free 0.293

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 2COL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1YRT Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of Bordetella pertussis in presence of c-terminal calmodulin Deposited 2005-02-04	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–364（364 aa） Fragment：Calmodulin-sensitive adenylate cyclase	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.6；298 K；PEG4000, Isopropanol, Sodium Citrate , pH 5.6, VAPOR DIFFUSION, temperature 298K	Resolution 2.10 Å R-free 0.270
1YRU Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of Bordetella pertussis in presence of c-terminal calmodulin and 1mM calcium chloride Deposited 2005-02-04	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–364（364 aa） Fragment：Calmodulin-sensitive adenylate cyclase	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；298 K；PEG2000, Tris, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.50 Å R-free 0.308
1ZOT crystal structure analysis of the CyaA/C-Cam with PMEAPP Deposited 2005-05-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–364（358 aa） Fragment：adenylyl cyclase toxin of Bordetella pertussis	Not recorded	MG MAGNESIUM ION × 3 EMA (ADENIN-9-YL-ETHOXYMETHYL)-HYDROXYPHOSPHINYL-DIPHOSPHATE × 1 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；277 K；PEG4000, Na Citrate, Propanol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277KK	Resolution 2.20 Å R-free 0.291

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

View Construct and Data Evidence

UniProt name	CYAA_BORPE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–356； UniProt 7–362

Calmodulin

Xenopus laevis

UniProt P62155

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 79–145	Not recorded	Bifunctional hemolysin-adenylate cyclase × 1 （P15318） MG MAGNESIUM ION × 2 POP PYROPHOSPHATE 2- × 1 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.6；278 K；PEG4000, Na Citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 278K	Resolution 2.20 Å R-free 0.293

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 2COL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CFC CALCIUM-FREE CALMODULIN Deposited 1995-08-02	Different construct Different oligomeric state 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 1–148（148 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1CFD CALCIUM-FREE CALMODULIN Deposited 1995-10-18	Different construct Different oligomeric state 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 1–148（148 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1CFF NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING PEPTIDE OF THE CA2+-PUMP Deposited 1999-03-18	Different construct 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 2–149（148 aa）	Not recorded	CA CALCIUM ION × 4	SOLUTION NMR NMR measurement conditions pH 6.5；303 K；Ionic strength (raw mmCIF value) 0.115；Pressure 1 NMR sample composition 90% H2O/10% D2O, 100% D2O	Resolution not provided
1DMO CALMODULIN, NMR, 30 STRUCTURES Deposited 1996-04-24	Different construct Different oligomeric state 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 1–148（148 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1F70 REFINED SOLUTION STRUCTURE OF CALMODULIN N-TERMINAL DOMAIN Deposited 2000-06-24	Different construct Different oligomeric state 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 2–76（75 aa） Fragment：N-TERMINAL DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100 mM KCL；Pressure ambient NMR sample composition 1 mM Calmodulin U-15N,13C; 5 mM Hepe buffer, 100 mM KCL \| 90% H2O/10% D2O NMR sample composition 1 mM Calmodulin U-15N,13C; 5 mM Hepe buffer, 100 mM KCL; 21 mg/ml filamentous phage Pf1 \| 90% H2O/10% D2O	Resolution not provided
1F71 REFINED SOLUTION STRUCTURE OF CALMODULIN C-TERMINAL DOMAIN Deposited 2000-06-24	Different construct Different oligomeric state 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 83–149（67 aa） Fragment：C-TERMINAL DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100mM KCl；Pressure ambient NMR sample composition 1 mM Calmodulin U-15N,13C; 5 mM Hepes buffer, 100 mM KCl \| 90% H2O/10% D2O NMR sample composition 1 mM Calmodulin U-15N,13C; 5 mM Hepes buffer, 100 mM KCl; 21 mg/ml filamentous phage pf1 \| 90% H2O/10% D2O	Resolution not provided
1IQ5 Calmodulin/nematode CA2+/Calmodulin dependent kinase kinase fragment Deposited 2001-06-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–149（149 aa）	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；ammonium sulfate, citratet, sodium tartrae, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å R-free 0.248
1MUX SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES Deposited 1997-09-06	Different construct Different oligomeric state 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 1–148（148 aa）	Not recorded	CA CALCIUM ION × 4 WW7 N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE × 2	SOLUTION NMR NMR measurement conditions pH 6.8；308 K；Ionic strength (raw mmCIF value) KCL, 100mM；Pressure 1	Resolution not provided
1NWD Solution Structure of Ca2+/Calmodulin bound to the C-terminal Domain of Petunia Glutamate Decarboxylase Deposited 2003-02-06	Different construct 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 A 1–148（148 aa）	Not recorded	CA CALCIUM ION × 4	SOLUTION NMR NMR measurement conditions pH 6.3；308 K；Ionic strength (raw mmCIF value) 100 mM KCl, 10 mM CaCl2 NMR sample composition 1 mM Calmodulin; 2.2 mM GAD \| 91% H2O, 9% D2O	Resolution not provided
1SY9 Structure of calmodulin complexed with a fragment of the olfactory CNG channel Deposited 2004-04-01	Different construct 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 1–148（148 aa）	Not recorded	CA CALCIUM ION × 4	SOLUTION NMR NMR measurement conditions pH 6.7；308 K NMR measurement conditions pH 6.7；308 K NMR sample composition 1.2 mM complex U-15N,13C, 6 mM CaCl2, 140 mM KCl, D2O \| D2O NMR sample composition 1.2 mM complex U-15N,13C, 6 mM CaCl2, 140 mM KCl, 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1X02 Solution structure of stereo array isotope labeled (SAIL) calmodulin Deposited 2005-03-11	Different construct Different oligomeric state 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 1–148（148 aa）	Not recorded	CA CALCIUM ION × 4	SOLUTION NMR NMR measurement conditions pH 6.5；310 K；Pressure AMBIENT NMR sample composition 0.7mM SAIL calmodulin, 5mM MES-d13, 10mM bis-Tris-d19, 5mM CaCl2, 0.1mM NaN3 \| 90% H2O/10% D2O	Resolution not provided
1Y0V Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate Deposited 2004-11-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 5–148（144 aa）	Not recorded	MG MAGNESIUM ION × 1 POP PYROPHOSPHATE 2- × 1 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；277 K；PEG400, MgCl2, Tris-HCl, pH 8.5, VAPOR DIFFUSION, temperature 277K	Resolution 3.60 Å R-free 0.307
1Y0V Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate Deposited 2004-11-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 5–148（144 aa）	Not recorded	MG MAGNESIUM ION × 1 POP PYROPHOSPHATE 2- × 1 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；277 K；PEG400, MgCl2, Tris-HCl, pH 8.5, VAPOR DIFFUSION, temperature 277K	Resolution 3.60 Å R-free 0.307
1Y0V Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate Deposited 2004-11-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain J 5–148（144 aa）	Not recorded	MG MAGNESIUM ION × 1 POP PYROPHOSPHATE 2- × 1 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；277 K；PEG400, MgCl2, Tris-HCl, pH 8.5, VAPOR DIFFUSION, temperature 277K	Resolution 3.60 Å R-free 0.307
1Y0V Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate Deposited 2004-11-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain K 5–148（144 aa）	Not recorded	MG MAGNESIUM ION × 1 POP PYROPHOSPHATE 2- × 1 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；277 K；PEG400, MgCl2, Tris-HCl, pH 8.5, VAPOR DIFFUSION, temperature 277K	Resolution 3.60 Å R-free 0.307
1Y0V Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate Deposited 2004-11-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 5–148（144 aa）	Not recorded	MG MAGNESIUM ION × 1 POP PYROPHOSPHATE 2- × 1 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；277 K；PEG400, MgCl2, Tris-HCl, pH 8.5, VAPOR DIFFUSION, temperature 277K	Resolution 3.60 Å R-free 0.307
1Y0V Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate Deposited 2004-11-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain M 5–148（144 aa）	Not recorded	MG MAGNESIUM ION × 1 POP PYROPHOSPHATE 2- × 1 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；277 K；PEG400, MgCl2, Tris-HCl, pH 8.5, VAPOR DIFFUSION, temperature 277K	Resolution 3.60 Å R-free 0.307
2I08 Solvation effect in conformational changes of EF-hand proteins: X-ray structure of Ca2+-saturated double mutant Q41L-K75I of N-domain of calmodulin Deposited 2006-08-10	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 1–78（78 aa） Fragment：N-DOMAIN OF CALMODULIN	Mutation：F19Y, Q41L, K75I, A1M, D78Y	CA CALCIUM ION × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；36% (v/v) PEG 400, 100 mM HEPES, 200 mM CaCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.00 Å R-free 0.243
2K3S HADDOCK-derived structure of the CH-domain of the smoothelin-like 1 complexed with the C-domain of apocalmodulin Deposited 2008-05-15	Different construct 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 83–149（67 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；293 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 0.5 mM [U-100% 15N] entity_1, 0.6 mM calmodulin (full length), 20 mM Bis-Tris, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 1 mM EDTA, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.6 mM entity_1, 0.5 mM [U-100% 15N] calmodulin (full length), 20 mM Bis-Tris, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 1 mM EDTA, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2KDU Structural basis of the Munc13-1/Ca2+-Calmodulin interaction: A novel 1-26 calmodulin binding motif with a bipartite binding mode Deposited 2009-01-19	Different construct 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 2–149（148 aa）	Not recorded	CA CALCIUM ION × 4	SOLUTION NMR NMR measurement conditions pH 6.8；308 K NMR sample composition 10 mM calcium, 1.5 mM [U-99% 13C; U-99% 15N] calmodulin, 1.8 mM Munc13-1, 150 mM potassium chloride, 20 mM BIS-TRIS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 10 mM calcium, 0.5 mM [U-99% 13C; U-99% 15N] Munc13-1, 0.6 mM calmodulin, 150 mM potassium chloride, 20 mM BIS-TRIS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 10 mM calcium, 1.5 mM [U-99% 13C; U-99% 15N] calmodulin, 1.8 mM Munc13, 150 mM potassium chloride, 20 mM BIS-TRIS, 100% D2O \| 100% D2O	Resolution not provided
2LLO Solution NMR-derived structure of calmodulin N-lobe bound with ER alpha peptide Deposited 2011-11-15	Different construct 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 2–81（80 aa） Fragment：EF-hand domains 1 and 2, residues 2-81	Not recorded	CA CALCIUM ION × 2	SOLUTION NMR NMR measurement conditions pH 7；310 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient NMR sample composition 1 mM [U-100% 13C; U-100% 15N] TRIS, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2LLQ Solution nmr-derived structure of calmodulin c-lobe bound with er alpha peptide Deposited 2011-11-15	Different construct 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 83–149（67 aa） Fragment：EF-hand domains 3 and 4, residues 83-149	Not recorded	CA CALCIUM ION × 2	SOLUTION NMR NMR measurement conditions pH 7；310 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient NMR sample composition 1 mM [U-100% 13C; U-100% 15N] protein, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
2MES Backbone 1H, 13C, 15N resonance assignments of calcium-bound calmodulin in complex with PSD95 N-terminal peptide Deposited 2013-09-26	Different construct 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 2–149（148 aa）	Not recorded	CA CALCIUM ION × 4	SOLUTION NMR NMR measurement conditions pH 7；310 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 400 uM [U-99% 13C; U-99% 15N] Calmodulin, PSD95NT, DTT, Tris, CaCl2, 600 uM PSD95_N-terminal_peptide, 20 mM Tris-d11, 50 mM NaCl, 5 mM CaCl2, 5 mM DTT-d, 93 % H2O, 7 % D2O, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
2RRT Solution structure of Magnesium-bound form of calmodulin C-domain E104D/E140D mutant Deposited 2011-04-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 79–149（71 aa） Fragment：C-terminal domain, UNP residues 79-149	Mutation：E28D, E64D	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；323 K；Ionic strength (raw mmCIF value) 0.5；Pressure ambient NMR sample composition 10 mM [U-2H] MES-1, 100 mM potassium chloride-2, 100 mM magnesium chloride-3, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
4R8G Crystal Structure of Myosin-1c tail in complex with Calmodulin Deposited 2014-09-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2–149（148 aa） Chain B 2–149（148 aa） Chain H 2–149（148 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；289.3 K；2.0M ammonium sulfate, 5% 1,4-dioxane, MES pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 289.3K	Resolution 3.50 Å R-free 0.304
5J7J NMR Derived Structure of Ca2+ Calmodulin bound to Phosphorylated PSD-95 Deposited 2016-04-06	Different construct 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 2–149（148 aa）	Not recorded	CA CALCIUM ION × 4	SOLUTION NMR NMR measurement conditions pH 7；318 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 500 uM [U-100% 13C; U-100% 15N] Calmodulin, 750 uM PSD-95 phosphorylated, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
5T0X Solution NMR-derived structure of calmodulin bound with ER alpha peptides Deposited 2016-08-16	Different construct 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 A 2–149（148 aa）	Not recorded	CA CALCIUM ION × 4	SOLUTION NMR NMR measurement conditions pH 7；310 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 1 mM [U-99% 15N] 15N-labeled CaM/ERalpha \| 90% H2O/10% D2O NMR sample composition 1 mM [U-99% 13C; U-99% 15N] 13C/15N-CaM/ERalpha \| 90% H2O/10% D2O NMR sample composition 1 mM [U-99% 13C; U-99% 15N] 13C/15N-CaM/ERalpha \| 100% D2O	Resolution not provided

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

View Construct and Data Evidence

UniProt name	CALM_XENLA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–67； UniProt 79–145

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	2col
Deposition date deposition_date	2005-05-18
Structure title title	Crystal structure analysis of CyaA/C-Cam with Pyrophosphate
Keywords keywords	LYASE, Calcium binding, LYASE-METAL BINDING PROTEIN COMPLEX; LYASE/METAL BINDING PROTEIN
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	26.42 Å
Radius of gyration Rg (electron density) rg_electron	26.01 Å
Forward intensity I(0) i0	39198900.00
Molecular weight molecular_weight	45943.0 kDa
Excluded volume excluded_volume	56433 Å³
Envelope volume envelope_volume	70120 Å³
Hydration-shell volume shell_volume	24418 Å³
Envelope diameter envelope_diameter	96.8 Å
Shell Rg shell_rg	31.08 Å
Envelope Rg envelope_rg	26.30 Å
Shape Rg shape_rg	26.02 Å
Total Rg total_rg	26.55 Å
Total atoms total_atoms	3227
Residues n_residues	416
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	93.9 Å
Rg (real space) rg_real	26.70 Å
Rg uncertainty (real space) rg_real_error	0.88 Å
I(0) (real space) i0_real	3.9200e+07
I(0) uncertainty (real space) i0_real_error	6.5180e+05
Rg (reciprocal space) rg_reciprocal	26.61 Å
I(0) (reciprocal space) i0_reciprocal	39200000.0000
Solution quality estimate total_estimate	0.8095
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	25.0 Å
Skewness Skewness skewness	0.640
Kurtosis Kurtosis kurtosis	-0.039
Angular range angular_range	— – 0.3000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11150000.0000
Real-space data points n_real_points	61
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.628; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.683; Smooth: 0.952

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Bifunctional hemolysin-adenylate cyclase
Molecular weight formula_weight	38562.9 kDa
EC 编号 ec_number	4.6.1.1
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3345

AGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEKIFVVSATGESQMLTRGQLKEYIGQQRGEGYVFYENRAYGVAGKSLFDDGL

来源 Source

来源生物 organism	Bordetella pertussis
NCBI Class编号 ncbi_taxonomy_id	520
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Calmodulin
Molecular weight formula_weight	7739.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

TDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMM

来源 Source

来源生物 organism	Xenopus laevis
通用名 common_name	African clawed frog
NCBI Class编号 ncbi_taxonomy_id	8355
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	PYROPHOSPHATE 2-
Molecular weight formula_weight	176.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	118

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7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2colb_
Class class	a — All alpha proteins
Fold Fold fold	a.39 — EF Hand-like
Superfamily Superfamily superfamily	a.39.1 — EF-hand
Family Family family	a.39.1.5 — Calmodulin-like

CATH v4.4 (4 domains)

Domain ID domain_id	2colA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	1720 —

Domain ID domain_id	2colA02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1760 — Adenylylcyclase toxin fold
Homologous superfamily homologous superfamily	10 — Anthrax toxin, edema factor, central domain

Domain ID domain_id	2colA03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	920 —

Domain ID domain_id	2colB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	238 — Recoverin; domain 1
Homologous superfamily homologous superfamily	10 — EF-hand

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8. Citations (1)

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Unit-cell length a length_a	79.613 Å
Unit-cell length b length_b	79.613 Å
Unit-cell length c length_c	139.465 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 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2470
R_work r_work	0.2400
R_free r_free	0.2930

fit	/app/data/saxs_computation/co/2col/2col.fit
pddf	/app/data/pr_computation/co/2col/2col.pr.out
profile	/app/data/saxs_computation/co/2col/2col.dat

Crystal structure analysis of CyaA/C-Cam with Pyrophosphate

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

Bifunctional hemolysin-adenylate cyclase

State in the Current Structure

Other States of the Same Protein in the Database

Calmodulin

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 (6)

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 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)