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- PDB-2cab: STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES... -

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Entry
Database: PDB / ID: 2cab
TitleSTRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I
ComponentsCARBONIC ANHYDRASE FORM B
KeywordsHYDRO-LYASE
Function / homology
Function and homology information


hydro-lyase activity / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / Reversible hydration of carbon dioxide / carbonic anhydrase / carbonate dehydratase activity / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen ...hydro-lyase activity / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / Reversible hydration of carbon dioxide / carbonic anhydrase / carbonate dehydratase activity / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / one-carbon metabolic process / extracellular exosome / zinc ion binding / cytosol
Similarity search - Function
Carbonic Anhydrase II / Alpha carbonic anhydrase / Carbonic anhydrase, alpha-class, conserved site / Alpha-carbonic anhydrases signature. / Carbonic anhydrase, alpha-class / Alpha carbonic anhydrase domain / Alpha carbonic anhydrase domain superfamily / Eukaryotic-type carbonic anhydrase / Alpha-carbonic anhydrases profile. / Eukaryotic-type carbonic anhydrase ...Carbonic Anhydrase II / Alpha carbonic anhydrase / Carbonic anhydrase, alpha-class, conserved site / Alpha-carbonic anhydrases signature. / Carbonic anhydrase, alpha-class / Alpha carbonic anhydrase domain / Alpha carbonic anhydrase domain superfamily / Eukaryotic-type carbonic anhydrase / Alpha-carbonic anhydrases profile. / Eukaryotic-type carbonic anhydrase / Roll / Alpha Beta
Similarity search - Domain/homology
Carbonic anhydrase 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / Resolution: 2 Å
AuthorsKannan, K.K. / Ramanadham, M. / Jones, T.A.
Citation
Journal: Ann.N.Y.Acad.Sci. / Year: 1984
Title: Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I
Authors: Kannan, K.K. / Ramanadham, M. / Jones, T.A.
#1: Journal: Biomolecular Structure, Conformation, Function and Evolution
Year: 1980
Title: Structure and Function of Carbonic Anhydrases
Authors: Kannan, K.K.
#2: Journal: Biophysics and Physiology of Carbon Dioxide / Year: 1980
Title: Crystal Structure of Carbonic Anhydrase
Authors: Kannan, K.K.
#3: Journal: Int.J.Quantum Chem.Quantum Chem.Symp. / Year: 1981
Title: Structure, Refinement, and Function of Human Carbonic Anhydrase-B
Authors: Kannan, K.K. / Ramanadham, M.
#4: Journal: FEBS Lett. / Year: 1977
Title: Structure and Function of Carbonic Anhydrases. Imidazole Binding to Human Carbonic Anhydrace B and the Mechanism of Action of Carbonic Anhydrases
Authors: Kannan, K.K. / Petef, M. / Fridborg, K. / Cid-Dresdner, H. / Lovgren, S.
#5: Journal: Proc.Natl.Acad.Sci.USA / Year: 1975
Title: Crystal Structure of Human Erythrocyte Carbonic Anhydrase B, Three-Dimensional Structure at a Nominal 2.2 Angstroms Resolution
Authors: Kannan, K.K. / Notstrand, B. / Fridborg, K. / Lovgren, S. / Ohlsson, A. / Petef, M.
#6: Journal: Isozymes-Molecular Structure / Year: 1975
Title: Structural Relationship of Human Erythrocyte Carbonic Anhydrase Isozymes B and C
Authors: Notstrand, B. / Vaara, I. / Kannan, K.K.
History
DepositionOct 5, 1983Processing site: BNL
SupersessionFeb 2, 1984ID: 1CAB
Revision 1.0Feb 2, 1984Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Feb 14, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

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Assembly

Deposited unit
A: CARBONIC ANHYDRASE FORM B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,8542
Polymers28,7891
Non-polymers651
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)81.500, 73.600, 37.100
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Atom site foot note1: RESIDUES 30 AND 202 ARE CIS-PROLINES. / 2: CYSTINE 212 IS MODIFIABLE BY MERCURIALS. / 3: HISTIDINE RESIDUES 94, 96 AND 119 ARE ZINC LIGANDS.
4: HISTIDINE RESIDUES 64, 67 AND 200 ARE IN THE ACTIVE SITE.
5: SEE REMARK 7.

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Components

#1: Protein CARBONIC ANHYDRASE FORM B


Mass: 28789.016 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P00915, carbonic anhydrase
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
Sequence detailsRESIDUE 74 IN THIS ENTRY IS IDENTIFIED AS GLN. HOWEVER, CHEMICAL SEQUENCE AND RECENT DIFFRACTION ...RESIDUE 74 IN THIS ENTRY IS IDENTIFIED AS GLN. HOWEVER, CHEMICAL SEQUENCE AND RECENT DIFFRACTION STUDIES ON AN INHIBITOR COMPLEX INDICATE THAT IT SHOULD BE ASP.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 1.93 Å3/Da / Density % sol: 36.26 %

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Processing

SoftwareName: CORELS / Classification: refinement
RefinementRfactor Rwork: 0.193 / Highest resolution: 2 Å
Details: HELICES E1 AND E2 WERE ASSIGNED DEFAULT TYPE 1 (ALPHA).
Refinement stepCycle: LAST / Highest resolution: 2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2009 0 1 0 2010

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