Complement component C2a, the catalytic fragment of C3- and C5-convertase of human complement. Determined by X-ray diffraction at 2.3 Å resolution. Released 6 Feb 2007.
Explore 2ODQ in 3D Show helices and sheets RCSB PDB PDBe
2ODQ contains 28 α-helices and 26 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 225-226 | 2 | 1 |
| β-strand | 232-240 | 9 | 2 |
| α-helix | 247-264 | 18 | |
| α-helix | 265-267 | 3 | |
| β-strand | 271-278 | 8 | 2 |
| β-strand | 282-286 | 5 | 2 |
| α-helix | 291-294 | 4 | |
| α-helix | 296-304 | 9 | |
| α-helix | 308-311 | 4 | |
| α-helix | 319-337 | 19 | |
| α-helix | 342-345 | 4 | |
| β-strand | 347-354 | 8 | 2 |
| α-helix | 365-375 | 11 | |
| α-helix | 380-385 | 6 | |
| β-strand | 386-393 | 8 | 2 |
| α-helix | 400-406 | 7 | |
| β-strand | 416-419 | 4 | 2 |
| α-helix | 422-432 | 11 | |
| β-strand | 433-434 | 2 | 1 |
| α-helix | 454-457 | 4 | |
| β-strand | 461-465 | 5 | 3 |
| β-strand | 472-476 | 5 | 3 |
| β-strand | 481-484 | 4 | 3 |
| α-helix | 486-488 | 3 | |
| β-strand | 499-502 | 4 | 3 |
| α-helix | 503 | 1 | |
| β-strand | 511-513 | 3 | 3 |
| β-strand | 515-520 | 6 | 3 |
| α-helix | 530-532 | 3 | |
| β-strand | 543-547 | 5 | 3 |
| α-helix | 550-553 | 4 | |
| β-strand | 554 | 1 | 4 |
| β-strand | 557 | 1 | 4 |
| α-helix | 559-560 | 2 | |
| β-strand | 561 | 1 | 5 |
| α-helix | 562 | 1 | |
| β-strand | 565 | 1 | 6 |
| α-helix | 566-571 | 6 | |
| α-helix | 580-587 | 8 | |
| β-strand | 592-598 | 7 | 5 |
| β-strand | 604-610 | 7 | 5 |
| α-helix | 613-620 | 8 | |
| α-helix | 621-624 | 4 | |
| α-helix | 635-637 | 3 | |
| β-strand | 643-646 | 4 | 5 |
| α-helix | 656-658 | 3 | |
| β-strand | 662-667 | 6 | 5 |
| β-strand | 670-680 | 11 | 5 |
| α-helix | 695-698 | 4 | |
| α-helix | 704-705 | 2 | |
| β-strand | 707-711 | 5 | 5 |
| α-helix | 712-714 | 3 | |
| α-helix | 716-723 | 8 | |
| β-strand | 729 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement C2 | A | protein | 509 | Homo sapiens | Q5JP69 (AlphaFold model) |
>2ODQ_1 Complement C2 (chains A) KIQIQRSGHLNLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSVAIITFASEPK VLMSVLNDNSRDMTEVISSLENANYKDHENGTGTNTYAALNSVYLMMNNQMRLLGMETMA WQEIRHAIILLTDGKSNMGGSPKTAVDHIREILNINQKRNDYLDIYAIGVGKLDVDWREL NELGSKKDGERHAFILQDTKALHQVFEHMLDVSKLTDTICGVGNMSANASDQERTPWHVT IKPKSQETCRGALISDQWVLTAAHCFRDGNDHSLWRVNVGDPKSQWGKEFLIEKAVISPG FDVFAKKNQGILEFYGDDIALLKLAQKVKMSTHARPICLPCTMEANLALRRPQGSTCRDH ENELLNKQSVPAHFVALNGSKLNINLKMGVEWTSCAEVVSQEKTMFPNLTDVREVVTDQF LCSGTQEDESPCKGESGGAVFLERRFRFFQVGLVSWGLYNPCLGSADKNSRKRAPRSKVP PPRDFHINLFRMQPWLRQHLGDVLNFLPL
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
The crystal structure of c2a, the catalytic fragment of classical pathway c3 and c5 convertase of human complement. Krishnan, V., Xu, Y., Macon, K. et al. J Mol Biol (2007) 367:224-233. DOI 10.1016/j.jmb.2006.12.039 · PubMed
Other PDB entries of the same protein (UniProt Q5JP69 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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