Beta Carbonic Anhydrase from the Carboxysomal Shell of Halothiobacillus neapolitanus (CsoSCA). Determined by X-ray diffraction at 2.2 Å resolution. Released 17 Jan 2006.
Explore 2FGY in 3D Show helices and sheets RCSB PDB PDBe
2FGY contains 55 α-helices and 30 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 56-74 | 19 | |
| α-helix | 76-85 | 10 | |
| α-helix | 87 | 1 | |
| α-helix | 93-104 | 12 | |
| α-helix | 110-112 | 3 | |
| β-strand | 116 | 1 | 1 |
| β-strand | 120 | 1 | 1 |
| α-helix | 123-141 | 19 | |
| α-helix | 152-163 | 12 | |
| β-strand | 165-172 | 8 | 2 |
| β-strand | 173 | 1 | 3 |
| α-helix | 176-178 | 3 | |
| α-helix | 181-186 | 6 | |
| α-helix | 188-190 | 3 | |
| β-strand | 194-196 | 3 | 2 |
| β-strand | 199 | 1 | 3 |
| α-helix | 200-202 | 3 | |
| α-helix | 206-223 | 18 | |
| β-strand | 234-243 | 10 | 2 |
| α-helix | 254-256 | 3 | |
| α-helix | 260-281 | 22 | |
| β-strand | 288-296 | 9 | 2 |
| β-strand | 301-305 | 5 | 2 |
| α-helix | 306-307 | 2 | |
| β-strand | 318-320 | 3 | 2 |
| α-helix | 321-328 | 8 | |
| α-helix | 333-348 | 16 | |
| α-helix | 352-354 | 3 | |
| α-helix | 362-386 | 25 | |
| α-helix | 390-391 | 2 | |
| α-helix | 392-394 | 3 | |
| β-strand | 401-405 | 5 | 4 |
| β-strand | 417-421 | 5 | 4 |
| α-helix | 426-428 | 3 | |
| α-helix | 429-442 | 14 | |
| α-helix | 444-446 | 3 | |
| β-strand | 450-458 | 9 | 4 |
| α-helix | 465-483 | 19 | |
| α-helix | 485-489 | 5 | |
| β-strand | 493-501 | 9 | 4 |
| α-helix | 506-507 | 2 | |
| β-strand | 508-511 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 56-74 | 19 | |
| α-helix | 76-85 | 10 | |
| α-helix | 87 | 1 | |
| α-helix | 93-104 | 12 | |
| α-helix | 110-113 | 4 | |
| β-strand | 116 | 1 | 5 |
| β-strand | 120 | 1 | 5 |
| α-helix | 123-141 | 19 | |
| α-helix | 152-162 | 11 | |
| β-strand | 165-172 | 8 | 6 |
| β-strand | 173 | 1 | 7 |
| α-helix | 176-178 | 3 | |
| α-helix | 181-185 | 5 | |
| α-helix | 188-190 | 3 | |
| β-strand | 194-196 | 3 | 6 |
| β-strand | 199 | 1 | 7 |
| α-helix | 200-202 | 3 | |
| α-helix | 206-223 | 18 | |
| β-strand | 234-243 | 10 | 6 |
| α-helix | 254-256 | 3 | |
| α-helix | 260-281 | 22 | |
| β-strand | 288-296 | 9 | 6 |
| β-strand | 301-305 | 5 | 6 |
| α-helix | 306-307 | 2 | |
| β-strand | 318-320 | 3 | 6 |
| α-helix | 321-328 | 8 | |
| α-helix | 333-347 | 15 | |
| α-helix | 352-354 | 3 | |
| α-helix | 359-361 | 3 | |
| α-helix | 362-386 | 25 | |
| α-helix | 390-391 | 2 | |
| α-helix | 392-394 | 3 | |
| β-strand | 401-405 | 5 | 8 |
| β-strand | 417-421 | 5 | 8 |
| α-helix | 429-442 | 14 | |
| α-helix | 444-446 | 3 | |
| α-helix | 448-449 | 2 | |
| β-strand | 450-458 | 9 | 8 |
| α-helix | 465-483 | 19 | |
| α-helix | 485-489 | 5 | |
| β-strand | 493-501 | 9 | 8 |
| α-helix | 506-507 | 2 | |
| β-strand | 508-511 | 4 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| carboxysome shell polypeptide | A, B | protein | 542 | Halothiobacillus neapolitanus | O85042 (AlphaFold model) |
>2FGY_1 carboxysome shell polypeptide (chains A, B) MSYYHHHHHHDYDIPTTENLYFQGAMGSMNTRNTRSKQRAPCGVSSSVKPRLDLIEQAPN PVYDRHPACITLPERTCRHPLTDLEANEQLGRCEDSVKNRFDRVIPFLQVVAGIPLGLDH VTRVQELAQSSLGHTLPEELLKDNWISGHNLKGIFGYATAKALTAATEQFSRKIMSEKDD SASAIGFFLDCGFHAVDISPCADGRLKGLLPYILRLPLTAFTYRKAYAGSMFDIEDDLAQ WEKNELRRYREGVPNTADQPTRYLKIAVYHFSTSDPTHSGCAAHGSNDRAALEAALTQLM KFREAVENAHCCGASIDILLIGVDTDTDAIRVHIPDSKGFLNPYRYVDNTVTYAQTLHLA PDEARVIIHEAILNANRSDGWAKGNGVASEGMRRFIGQLLINNLSQIDYVVNRHGGRYPP NDIGHAERYISVGDGFDEVQIRNLAYYAHLDTVEENAIDVDVGITIFTKLNLSRGLPIPI AIHYRYDPNVPGSRERTVVKARRIYNAIKERFSSLDEQNLLQFRLSVQAQDIGSPIEEVA SA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
The Structure of beta-carbonic anhydrase from the carboxysomal shell reveals a distinct subclass with one active site for the price of two. Sawaya, M.R., Cannon, G.C., Heinhorst, S. et al. J Biol Chem (2006) 281:7546-7555. DOI 10.1074/jbc.M510464200 · PubMed
Other PDB entries of the same protein (UniProt O85042 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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