SAXSdb — 6skt

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

Carbonic anhydrase 2

OrganismNot specified

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 1–260	Not recorded	CU COPPER (II) ION × 2 ZN ZINC ION × 1 GOL GLYCEROL × 1 E6B ~{N}-[2-(1~{H}-imidazol-4-yl)ethyl]-4-sulfamoyl-benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；100mM HEPES pH7.5, 14% PEG3350, 20% Glycerol, 5mM CuCl2	Resolution 1.90 Å R-free 0.204

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 6SKT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1G6V Complex of the camelid heavy-chain antibody fragment CAB-CA05 with bovine carbonic anhydrase Deposited 2000-11-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 0–260（261 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；PEG 8000, sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.50 Å R-free 0.276
1V9E Crystal Structure Analysis of Bovine Carbonic Anhydrase II Deposited 2004-01-26	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–259（259 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；pH 7.5；277 K；50mM Tris-HCl, 2.4M Ammonium sulfate, pH 7.5, SMALL TUBES, temperature 277K	Resolution 1.95 Å R-free 0.298
1V9E Crystal Structure Analysis of Bovine Carbonic Anhydrase II Deposited 2004-01-26	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–259（259 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；pH 7.5；277 K；50mM Tris-HCl, 2.4M Ammonium sulfate, pH 7.5, SMALL TUBES, temperature 277K	Resolution 1.95 Å R-free 0.298
1V9I Crystal Structure Analysis of the site specific mutant (Q253C) of bovine carbonic anhydrase II Deposited 2004-01-26	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 C 1–259（259 aa）	Mutation：Q253C	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；pH 7.5；277 K；50mM Tris-HCl, 3mM NaN3, 2.3M Ammonium Sulfate, pH 7.5, SMALL TUBES, temperature 277K	Resolution 2.95 Å R-free 0.346
23OM Crystal Structure Analysis of Bovine Carbonic Anhydrase II to 5-(2-morpholin-4-ylcarbonyl-1,3-oxazol-5-yl)thiophene-2-sulfonamide. Deposited 2026-02-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–260（259 aa）	Not recorded	8V5 5-(2-morpholin-4-ylcarbonyl-1,3-oxazol-5-yl)thiophene-2-sulfonamide × 1 BOG octyl beta-D-glucopyranoside × 1 GOL GLYCEROL × 3 ZN ZINC ION × 1 ACT ACETATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；2M ammonium sulfate, 0.1M Tris base Buffer	Resolution 1.70 Å R-free 0.250
23OM Crystal Structure Analysis of Bovine Carbonic Anhydrase II to 5-(2-morpholin-4-ylcarbonyl-1,3-oxazol-5-yl)thiophene-2-sulfonamide. Deposited 2026-02-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–260（259 aa）	Not recorded	8V5 5-(2-morpholin-4-ylcarbonyl-1,3-oxazol-5-yl)thiophene-2-sulfonamide × 1 BOG octyl beta-D-glucopyranoside × 1 GOL GLYCEROL × 3 ZN ZINC ION × 1 ACT ACETATE ION × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；2M ammonium sulfate, 0.1M Tris base Buffer	Resolution 1.70 Å R-free 0.250
23ON Crystal Structure Analysis of Bovine Carbonic Anhydrase II to 4-2-methyl-1,3-oxazol-5-ylbenzenesulfonamide Deposited 2026-02-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–260（259 aa）	Not recorded	8V8 4-(2-methyl-1,3-oxazol-5-yl)benzenesulfonamide × 1 GOL GLYCEROL × 3 ACT ACETATE ION × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；2M ammonium sulfate, 0.1M Tris-base Buffer	Resolution 1.50 Å R-free 0.200
23ON Crystal Structure Analysis of Bovine Carbonic Anhydrase II to 4-2-methyl-1,3-oxazol-5-ylbenzenesulfonamide Deposited 2026-02-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–260（259 aa）	Not recorded	8V8 4-(2-methyl-1,3-oxazol-5-yl)benzenesulfonamide × 1 GOL GLYCEROL × 3 ACT ACETATE ION × 2 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；2M ammonium sulfate, 0.1M Tris-base Buffer	Resolution 1.50 Å R-free 0.200
4CNR Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture Deposited 2014-01-24	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 1–260（260 aa）	Mutation：YES	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；281 K；10 MG/ML PROTEIN WITH 30% PEG 1500 AT 8C, pH 5.5	Resolution 2.29 Å R-free 0.236
4CNR Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture Deposited 2014-01-24	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–260（260 aa）	Mutation：YES	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；281 K；10 MG/ML PROTEIN WITH 30% PEG 1500 AT 8C, pH 5.5	Resolution 2.29 Å R-free 0.236
4CNR Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture Deposited 2014-01-24	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1–260（260 aa）	Mutation：YES	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；281 K；10 MG/ML PROTEIN WITH 30% PEG 1500 AT 8C, pH 5.5	Resolution 2.29 Å R-free 0.236
4CNR Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture Deposited 2014-01-24	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1–260（260 aa）	Mutation：YES	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；281 K；10 MG/ML PROTEIN WITH 30% PEG 1500 AT 8C, pH 5.5	Resolution 2.29 Å R-free 0.236
4CNV Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture Deposited 2014-01-25	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 1–260（260 aa）	Mutation：YES	ZN ZINC ION × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；PROTEIN WAS AT 10 MG/ML; THE RESERVOIR SOLUTION WAS 5% PEG 1000, 30% PEG 600, 10% GLYCEROL, 100 MM SODIUM MES BUFFER AT PH 6. SEEDS OF THE MUT1 FORM WERE USED TO OBTAIN THESE CRYSTALS.	Resolution 1.62 Å R-free 0.182
4CNW Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture Deposited 2014-01-25	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 1–260（260 aa）	Mutation：YES	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN WAS AT 10 MG/ML. THE RESERVOIR CONDITIONS WERE: 25% PEG MME 2000, 200 MM CALCIUM ACETATE, 50 MM TRIS BUFFER PH 8.0. THE CRYSTALS WERE OBTAINED THROUGH CROSS SEEDING FROM A DIFFERENT MUTANT CA-II CRYSTAL.	Resolution 2.03 Å R-free 0.259
4CNW Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture Deposited 2014-01-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–260（260 aa）	Mutation：YES	ZN ZINC ION × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；PROTEIN WAS AT 10 MG/ML. THE RESERVOIR CONDITIONS WERE: 25% PEG MME 2000, 200 MM CALCIUM ACETATE, 50 MM TRIS BUFFER PH 8.0. THE CRYSTALS WERE OBTAINED THROUGH CROSS SEEDING FROM A DIFFERENT MUTANT CA-II CRYSTAL.	Resolution 2.03 Å R-free 0.259
4CNX Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture Deposited 2014-01-25	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 1–260（260 aa）	Mutation：YES	ZN ZINC ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.5；281 K；PROTEIN WAS AT 10 MG/ML. THE RESERVOIR CONDITIONS WERE: 40% PEG 600, 100 MM SODIUM CITRATE AT PH 5.5 SET UP AT 8C. CROSS SEEDING FROM OTHER MUTANT CA-II CRYSTALS WAS USED TO OBTAIN THESE CRYSTALS.	Resolution 1.23 Å R-free 0.147
5A25 Rational engineering of a mesophilic carbonic anhydrase to an extreme halotolerant biocatalyst Deposited 2015-05-12	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–260（260 aa）	Not recorded	ZN ZINC ION × 1 GOL GLYCEROL × 1 NA SODIUM ION × 2 BOG octyl beta-D-glucopyranoside × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.2；150 NL 20 MG/ML PROTEIN PLUS 150 NL RESERVOIR CONSISTING OF 50 MM TRIS PH 8.2, 2.3 M AMMONIUM SULFATE, 0.023 (W/V) N-OCTYL-B-D-GLUCOPYRANOSIDE	Resolution 1.90 Å R-free 0.197
5A25 Rational engineering of a mesophilic carbonic anhydrase to an extreme halotolerant biocatalyst Deposited 2015-05-12	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–260（260 aa）	Not recorded	ZN ZINC ION × 1 NA SODIUM ION × 2 BOG octyl beta-D-glucopyranoside × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.2；150 NL 20 MG/ML PROTEIN PLUS 150 NL RESERVOIR CONSISTING OF 50 MM TRIS PH 8.2, 2.3 M AMMONIUM SULFATE, 0.023 (W/V) N-OCTYL-B-D-GLUCOPYRANOSIDE	Resolution 1.90 Å R-free 0.197
5EZT Peracetylated Bovine Carbonic Anhydrase II Deposited 2015-11-26	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 X 4–260（257 aa） Fragment：UNP residues 4-260	Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277.15 K；1.6M ammonium sulfate, tris	Resolution 1.54 Å R-free 0.239
6SKS Crystal structure of bovine carbonic anhydrase II in complex with a benzenesulfonamide-based ligand (SH1) Deposited 2019-08-16	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–260（260 aa）	Not recorded	CU COPPER (II) ION × 4 ZN ZINC ION × 1 GOL GLYCEROL × 2 E68 ~{N}-[2-[2-(1~{H}-imidazol-4-yl)ethylamino]-2-oxidanylidene-ethyl]-4-sulfamoyl-benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；100mM HEPES pH7.5, 14% PEG3350, 20% Glycerol, 5mM CuCl2	Resolution 1.75 Å R-free 0.194
6SKV Crystal structure of bovine carbonic anhydrase II in complex with a benzenesulfonamide-based ligand (SH2) Deposited 2019-08-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–260（260 aa）	Not recorded	ZN ZINC ION × 1 CU COPPER (II) ION × 3 GOL GLYCEROL × 2 E5Z ~{N}-[3-[(~{E})-2-(1~{H}-imidazol-5-yl)ethylideneamino]-3-oxidanylidene-propyl]-4-sulfamoyl-benzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；100mM HEPES pH7.5, 14% PEG3350, 20% Glycerol, 5mM CuCl2.	Resolution 1.75 Å R-free 0.189

13 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CAH2_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–260； UniProt 1–260

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	6skt
Deposition date deposition_date	2019-08-16
Structure title title	Crystal structure of bovine carbonic anhydrase II in complex with a benzenesulfonamide-based ligand (SH0)
Keywords keywords	CARBONIC ANHYDRASE II, CA2, SULFONAMIDE, COMPLEX, LYASE; LYASE
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	18.47 Å
Radius of gyration Rg (electron density) rg_electron	17.27 Å
Forward intensity I(0) i0	15561200.00
Molecular weight molecular_weight	29471.0 kDa
Excluded volume excluded_volume	36709 Å³
Envelope volume envelope_volume	40722 Å³
Hydration-shell volume shell_volume	19114 Å³
Envelope diameter envelope_diameter	59.5 Å
Shell Rg shell_rg	24.05 Å
Envelope Rg envelope_rg	17.63 Å
Shape Rg shape_rg	17.24 Å
Total Rg total_rg	18.35 Å
Total atoms total_atoms	2077
Residues n_residues	258
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	57.7 Å
Rg (real space) rg_real	18.33 Å
Rg uncertainty (real space) rg_real_error	0.34 Å
I(0) (real space) i0_real	1.5560e+07
I(0) uncertainty (real space) i0_real_error	1.8240e+05
Rg (reciprocal space) rg_reciprocal	18.35 Å
I(0) (reciprocal space) i0_reciprocal	15560000.0000
Solution quality estimate total_estimate	0.8112
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	23.7 Å
Skewness Skewness skewness	0.062
Kurtosis Kurtosis kurtosis	-0.465
Angular range angular_range	— – 0.4300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2750000.0000
Real-space data points n_real_points	74
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.855; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.000

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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	Carbonic anhydrase 2
Molecular weight formula_weight	29151.8 kDa
EC 编号 ec_number	4.2.1.1
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2252

MSHHWGYGKHNGPEHWHKDFPIANGERQSPVDIDTKAVVQDPALKPLALVYGEATSRRMVNNGHSFNVEYDDSQDKAVLKDGPLTGTYRLVQFHFHWGSSDDQGSEHTVDRKKYAAELHLVHWNTKYGDFGTAAQQPDGLAVVGVFLKVGDANPALQKVLDALDSIKTKGKSTDFPNFDPGSLLPNVLDYWTYPGSLTTPPLLESVTWIVLKEPISVSSQQMLKFRTLNFNAEGEPELLMLANWRPAQPLKNRQVRGFPK

Entity 2 Entity 2 non-polymer

Description description	COPPER (II) ION
Molecular weight formula_weight	63.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	~{N}-[2-(1~{H}-imidazol-4-yl)ethyl]-4-sulfamoyl-benzamide
Molecular weight formula_weight	294.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	175

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d6skta_
Class class	b — All beta proteins
Fold Fold fold	b.74 — Carbonic anhydrase
Superfamily Superfamily superfamily	b.74.1 — Carbonic anhydrase
Family Family family	b.74.1.1 — Carbonic anhydrase

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8. Citations (1)

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Unit-cell length a length_a	67.619 Å
Unit-cell length b length_b	67.619 Å
Unit-cell length c length_c	123.429 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	42.400 Å
R factor r_factor	0.1784
R_work r_work	0.1771
R_free r_free	0.2043

fit	/app/data/saxs_computation/sk/6skt/6skt.fit
pddf	/app/data/pr_computation/sk/6skt/6skt.pr.out
profile	/app/data/saxs_computation/sk/6skt/6skt.dat

Crystal structure of bovine carbonic anhydrase II in complex with a benzenesulfonamide-based ligand (SH0)

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

Carbonic anhydrase 2

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