SAXSdb — 1cdn

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

CALBINDIN D9K

Bos taurus

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 4–78	Mutation：INS(MET 1), P43G	No other associated polymer	SOLUTION NMR mmCIF provides none of the parsed experimental conditions	Resolution not provided

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 1CDN	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B1G SOLVATED REFINEMENT OF CA-LOADED CALBINDIN D9K Deposited 1998-11-20	Different mutation/modification Different ligand/ion	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4–78（75 aa）	Mutation：P43G	CA CALCIUM ION × 2	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1BOC THE SOLUTION STRUCTURES OF MUTANT CALBINDIN D9K'S, AS DETERMINED BY NMR, SHOW THAT THE CALCIUM BINDING SITE CAN ADOPT DIFFERENT FOLDS Deposited 1993-04-23	Different mutation/modification	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4–78（75 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1BOD THE SOLUTION STRUCTURES OF MUTANT CALBINDIN D9K'S, AS DETERMINED BY NMR, SHOW THAT THE CALCIUM BINDING SITE CAN ADOPT DIFFERENT FOLDS Deposited 1993-04-23	Different mutation/modification	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4–78（75 aa）	Mutation：A15D,P20G,P43M	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1CLB Determination of the solution structure of apo calbindin D9K by nmr spectroscopy Deposited 1995-02-08	Different mutation/modification	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4–78（75 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1D1O COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEINS: EVIDENCE OF SITE-SITE COMMUNICATION FROM BINDING-INDUCED CHANGES IN STRUCTURE AND DYNAMICS OF N56A CALBINDIN D9K Deposited 1999-09-20	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 5–79（75 aa） Fragment：CALBINDIN D9K	Mutation：P43M, N56A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) 0；Pressure AMBIENT NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) 0；Pressure AMBIENT NMR sample composition 4 MM N56A-CALBINDIN D9K NMR sample composition 4 MM 15N-LABELED N56A-CALBINDIN D9K;	Resolution not provided
1HT9 DOMAIN SWAPPING EF-HANDS Deposited 2000-12-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 4–78（75 aa） Chain B 4–78（75 aa）	Mutation：YES Mutation：YES	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；293 K；ammonium sulphate, calcium chloride, magnesium chloride, EVAPORATION, temperature 293K	Resolution 1.76 Å R-free 0.192
1IG5 BOVINE CALBINDIN D9K BINDING MG2+ Deposited 2001-04-17	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 4–78（75 aa）	Not recorded	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.4；298 K；3M ammonium sulphate, 100 mM magnesium chloride, pH 6.4, EVAPORATION, temperature 298K	Resolution 1.50 Å R-free 0.285
1IGV BOVINE CALBINDIN D9K BINDING MN2+ Deposited 2001-04-18	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 4–78（75 aa）	Not recorded	MN MANGANESE (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.6；295 K；65 % ammonium sulphate, 600 mM MnCl2, pH 5.6, EVAPORATION, temperature 295K	Resolution 1.85 Å R-free 0.272
1KCY NMR solution structure of apo calbindin D9k (F36G + P43M mutant) Deposited 2001-11-12	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4–78（75 aa） Fragment：contains EF-HAND 1 (LOW AFFINITY) and EF-HAND 2 (HIGH AFFINITY)	Mutation：F36G, P43M	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) no added salts；Pressure ambient NMR sample composition 2.5 mM calbindin; 95% H2O; 5% D2O \| 95% H20; 5% D2O NMR sample composition 2.5 mM calbindin D9k U-15N; 95% H2O; 5% D2O \| 95% H2O/5% D2O NMR sample composition 2.5 mM calbindin D9k; 100% D20 \| 100% D2O	Resolution not provided
1KQV Family of NMR Solution Structures of Ca Ln Calbindin D9K Deposited 2002-01-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 0–78（79 aa）	Mutation：P43M	LA LANTHANUM (III) ION × 1	SOLUTION NMR NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) water solution；Pressure 1 NMR measurement conditions pH 6；283 K；Ionic strength (raw mmCIF value) water solution；Pressure 1 NMR sample composition 2.0 mM Ca Ln Cb \| H2O/D2O 10:1	Resolution not provided
1KSM AVERAGE NMR SOLUTION STRUCTURE OF CA LN CALBINDIN D9K Deposited 2002-01-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 0–78（79 aa）	Mutation：P43M	LA LANTHANUM (III) ION × 1	SOLUTION NMR NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) WATER SOLUTION；Pressure AMBIENT NMR sample composition 1.5 MM [15N, 13C] - CA LN CALBINDIN, PH 6.0 \| H20:D2O 90:10	Resolution not provided
1N65 FAMILY OF NMR SOLUTION STRUCTURES OF CA CE CALBINDIN D9K IN DENATURATING CONDITIONS Deposited 2002-11-08	Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4–78（75 aa）	Mutation：P43M	CE CERIUM (III) ION × 1	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 2M Guanidinium Chloride (GmdHCl)；Pressure 1 NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) pure water；Pressure 1 NMR sample composition Uniform labeling with 15N, H2O/D20 90/10 \| H2O/D20 90/10 Denaturating Conditions NMR sample composition Uniform labeling with 15N, H2O/D20 90/10 \| H2O/D20 90/10	Resolution not provided
1QX2 X-ray Structure of Calcium-loaded Calbindomodulin (A Calbindin D9k Re-engineered to Undergo a Conformational Opening) at 1.44 A Resolution Deposited 2003-09-04	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 4–78（75 aa）	Mutation：L6I, I9A, K12V, Y13F, L23I, L31V, L32M, E35L, F36G, L49M, F50I, L53V, Q67L, L69M, V70M, P43M Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；PEG 550 MME, MES, zinc sulfate, Tris-HCl, sodium chloride, calcium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.44 Å R-free 0.194
1QX2 X-ray Structure of Calcium-loaded Calbindomodulin (A Calbindin D9k Re-engineered to Undergo a Conformational Opening) at 1.44 A Resolution Deposited 2003-09-04	Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 4–78（75 aa）	Mutation：L6I, I9A, K12V, Y13F, L23I, L31V, L32M, E35L, F36G, L49M, F50I, L53V, Q67L, L69M, V70M, P43M Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；PEG 550 MME, MES, zinc sulfate, Tris-HCl, sodium chloride, calcium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.44 Å R-free 0.194
1QX2 X-ray Structure of Calcium-loaded Calbindomodulin (A Calbindin D9k Re-engineered to Undergo a Conformational Opening) at 1.44 A Resolution Deposited 2003-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 4–78（75 aa） Chain B 4–78（75 aa）	Mutation：L6I, I9A, K12V, Y13F, L23I, L31V, L32M, E35L, F36G, L49M, F50I, L53V, Q67L, L69M, V70M, P43M Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L6I, I9A, K12V, Y13F, L23I, L31V, L32M, E35L, F36G, L49M, F50I, L53V, Q67L, L69M, V70M, P43M Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 4 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；PEG 550 MME, MES, zinc sulfate, Tris-HCl, sodium chloride, calcium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.44 Å R-free 0.194
1QX2 X-ray Structure of Calcium-loaded Calbindomodulin (A Calbindin D9k Re-engineered to Undergo a Conformational Opening) at 1.44 A Resolution Deposited 2003-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 4–78（75 aa） Chain B 4–78（75 aa）	Mutation：L6I, I9A, K12V, Y13F, L23I, L31V, L32M, E35L, F36G, L49M, F50I, L53V, Q67L, L69M, V70M, P43M Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L6I, I9A, K12V, Y13F, L23I, L31V, L32M, E35L, F36G, L49M, F50I, L53V, Q67L, L69M, V70M, P43M Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 4 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；PEG 550 MME, MES, zinc sulfate, Tris-HCl, sodium chloride, calcium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.44 Å R-free 0.194
1QX2 X-ray Structure of Calcium-loaded Calbindomodulin (A Calbindin D9k Re-engineered to Undergo a Conformational Opening) at 1.44 A Resolution Deposited 2003-09-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 4–78（75 aa） Chain B 4–78（75 aa）	Mutation：L6I, I9A, K12V, Y13F, L23I, L31V, L32M, E35L, F36G, L49M, F50I, L53V, Q67L, L69M, V70M, P43M Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：L6I, I9A, K12V, Y13F, L23I, L31V, L32M, E35L, F36G, L49M, F50I, L53V, Q67L, L69M, V70M, P43M Non-standard monomer：Yes (specific site not provided by mmCIF)	CA CALCIUM ION × 4 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；PEG 550 MME, MES, zinc sulfate, Tris-HCl, sodium chloride, calcium chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.44 Å R-free 0.194
1RT0 12-mer from site II calbindin D9K (DKNGDGEVSFEE) coordinating Zn(II) Deposited 2003-12-10	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 57–68（12 aa） Fragment：residues 57-68 (SWS P02632)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；288 K；Ionic strength (raw mmCIF value) aprox 0；Pressure ambient NMR sample composition 3mM Peptide and Zn(NO3)2. NaOH and HNO3 added for pH fixing to 7; 80% H2O, 20% D2O \| 80% H2O, 20% D2O	Resolution not provided
2BCA HIGH-RESOLUTION SOLUTION STRUCTURE OF CALCIUM-LOADED CALBINDIN D9K Deposited 1993-08-18	Different mutation/modification	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4–78（75 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
2BCB HIGH-RESOLUTION SOLUTION STRUCTURE OF CALCIUM-LOADED CALBINDIN D9K Deposited 1993-08-18	Different mutation/modification	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4–78（75 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
2MAZ Backbone 1H, 13C, and 15N Chemical Shift Assignments for Bovine Apo Calbindin Deposited 2013-07-22	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 5–79（75 aa） Fragment：UNP residues 5-79	Mutation：P43M	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.2；298 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient NMR sample composition 1mM [U-100% 13C; U-100% 15N] D2O-1, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3ICB THE REFINED STRUCTURE OF VITAMIN D-DEPENDENT CALCIUM-BINDING PROTEIN FROM BOVINE INTESTINE. MOLECULAR DETAILS, ION BINDING, AND IMPLICATIONS FOR THE STRUCTURE OF OTHER CALCIUM-BINDING PROTEINS Deposited 1986-09-09	Different mutation/modification Different ligand/ion Different experimental method Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4–78（75 aa）	Not recorded	CA CALCIUM ION × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
4ICB PROLINE CIS-TRANS ISOMERS IN CALBINDIN D9K OBSERVED BY X-RAY CRYSTALLOGRAPHY Deposited 1991-08-27	Different mutation/modification Different ligand/ion Different experimental method Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 4–78（75 aa）	Not recorded	CA CALCIUM ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.60 Å

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

View Construct and Data Evidence

UniProt name	S100G_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–76； UniProt 4–78

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	1cdn
Deposition date deposition_date	1995-08-04
Structure title title	Solution structure of (CD2+)1-calbindin D9K reveals details of the stepwise structural changes along the apo--> (CA2+)II1--> (CA2+)I,II2 binding pathway
Keywords keywords	EF-HAND, CALCIUM-BINDING PROTEIN; CALCIUM-BINDING PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	11.57 Å
Radius of gyration Rg (electron density) rg_electron	11.14 Å
Forward intensity I(0) i0	525634000.00
Molecular weight molecular_weight	202880.0 kDa
Excluded volume excluded_volume	257110 Å³
Envelope volume envelope_volume	17070 Å³
Hydration-shell volume shell_volume	11337 Å³
Envelope diameter envelope_diameter	39.7 Å
Shell Rg shell_rg	18.65 Å
Envelope Rg envelope_rg	12.92 Å
Shape Rg shape_rg	11.11 Å
Total Rg total_rg	11.39 Å
Total atoms total_atoms	28632
Residues n_residues	1800
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	34.7 Å
Rg (real space) rg_real	11.45 Å
Rg uncertainty (real space) rg_real_error	0.19 Å
I(0) (real space) i0_real	5.2560e+08
I(0) uncertainty (real space) i0_real_error	5.3240e+06
Rg (reciprocal space) rg_reciprocal	11.45 Å
I(0) (reciprocal space) i0_reciprocal	525600000.0000
Solution quality estimate total_estimate	0.8808
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	16.3 Å
Skewness Skewness skewness	-0.209
Kurtosis Kurtosis kurtosis	-0.416
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	61590.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.827; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.995

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1cdna_
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.39.1.1 — Calbindin D9K

CATH v4.4 (1 domains)

Domain ID domain_id	1cdnA00
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 (4)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

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

Description description	CALBINDIN D9K
Molecular weight formula_weight	8601.7 kDa
Mutation mutation	INS(MET 1), P43G
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	28632

来源生物 organism	Bos taurus
通用名 common_name	cattle
NCBI Class编号 ncbi_taxonomy_id	9913
宿主生物 host_organism	Escherichia coli

Solution structure of (CD2+)1-calbindin D9K reveals details of the stepwise structural changes along the apo--> (CA2+)II1--> (CA2+)I,II2 binding pathway

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

CALBINDIN D9K

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/cd/1cdn/1cdn.fit
pddf	/app/data/pr_computation/cd/1cdn/1cdn.pr.out
profile	/app/data/saxs_computation/cd/1cdn/1cdn.dat