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4cnx

Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture

Method: X-RAY DIFFRACTION Dmax: 59.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CARBONIC ANHYDRASE 2

BOS TAURUS

UniProt P00921

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 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

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 4CNX 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 mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 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 mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–259（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 mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–259（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 mutation/modification 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 mutation/modification 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 mutation/modification 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 mutation/modification 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 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 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 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 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 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 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 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
5A25 Rational engineering of a mesophilic carbonic anhydrase to an extreme halotolerant biocatalyst Deposited 2015-05-12 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）
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 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）
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 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）
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
6SKT Crystal structure of bovine carbonic anhydrase II in complex with a benzenesulfonamide-based ligand (SH0) Deposited 2019-08-16 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）
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
6SKV Crystal structure of bovine carbonic anhydrase II in complex with a benzenesulfonamide-based ligand (SH2) Deposited 2019-08-16 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）
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 3–262； 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.

SAXS scattering curve SAXS Profile

SAXS profile for 4cnx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4cnx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4cnx
Deposition date deposition_date2014-01-25
Structure title titleSurface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture
Keywords keywordsLYASE, PROTEIN ENGINEERING, CO2 CAPTURE; LYASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier18.56 Å
Radius of gyration Rg (electron density) rg_electron17.23 Å
Forward intensity I(0) i015325900.00
Molecular weight molecular_weight28995.0 kDa
Excluded volume excluded_volume35964 ų
Envelope volume envelope_volume40054 ų
Hydration-shell volume shell_volume18893 ų
Envelope diameter envelope_diameter59.4 Å
Shell Rg shell_rg23.90 Å
Envelope Rg envelope_rg17.53 Å
Shape Rg shape_rg17.21 Å
Total Rg total_rg18.24 Å
Total atoms total_atoms2051
Residues n_residues257
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax59.9 Å
Rg (real space) rg_real18.41 Å
Rg uncertainty (real space) rg_real_error0.38 Å
I(0) (real space) i0_real1.5330e+07
I(0) uncertainty (real space) i0_real_error2.0160e+05
Rg (reciprocal space) rg_reciprocal18.43 Å
I(0) (reciprocal space) i0_reciprocal15330000.0000
Solution quality estimate total_estimate0.8047
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.6 Å
Skewness Skewness skewness0.043
Kurtosis Kurtosis kurtosis-0.479
Angular range angular_range— – 0.4300 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2923000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.823; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4cnxa_
Class classb — All beta proteins
Fold Fold foldb.74 — Carbonic anhydrase
Superfamily Superfamily superfamilyb.74.1 — Carbonic anhydrase
Family Family familyb.74.1.1 — Carbonic anhydrase

CATH v4.4 (1 domains)

Domain ID domain_id4cnxA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology200 — Carbonic Anhydrase II
Homologous superfamily homologous superfamily10 — Alpha carbonic anhydrase
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8. Citations (1)

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9. Files and Curves (10)