Clavulanic acid biosynthesis oligopeptide binding protein 2 complexed with bradykinin. Determined by X-ray diffraction at 1.7 Å resolution. Released 8 Dec 2009.
Explore 2WOK in 3D Show helices and sheets RCSB PDB PDBe
2WOK contains 30 α-helices and 31 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 |
|---|---|---|---|
| α-helix | 9-11 | 3 | |
| β-strand | 25 | 1 | 1 |
| β-strand | 34-39 | 6 | 2 |
| α-helix | 54-63 | 10 | |
| β-strand | 68-69 | 2 | 3 |
| α-helix | 76-79 | 4 | |
| β-strand | 82-83 | 2 | 3 |
| β-strand | 86 | 1 | 4 |
| α-helix | 90 | 1 | |
| β-strand | 91-93 | 3 | 5 |
| α-helix | 94-96 | 3 | |
| β-strand | 98-102 | 5 | 5 |
| β-strand | 103 | 1 | 4 |
| α-helix | 104 | 1 | |
| β-strand | 108 | 1 | 6 |
| α-helix | 113 | 1 | |
| β-strand | 114 | 1 | 6 |
| α-helix | 115 | 1 | |
| α-helix | 117-126 | 10 | |
| α-helix | 140-144 | 5 | |
| β-strand | 146 | 1 | 7 |
| β-strand | 149 | 1 | 7 |
| α-helix | 160-161 | 2 | |
| β-strand | 164-168 | 5 | 5 |
| β-strand | 171-175 | 5 | 5 |
| α-helix | 183-187 | 5 | |
| α-helix | 190-192 | 3 | |
| α-helix | 197-199 | 3 | |
| α-helix | 202-207 | 6 | |
| β-strand | 215-221 | 7 | 2 |
| β-strand | 225-230 | 6 | 2 |
| α-helix | 236-238 | 3 | |
| β-strand | 248-253 | 6 | 2 |
| α-helix | 257-265 | 9 | |
| β-strand | 271-272 | 2 | 2 |
| α-helix | 280-288 | 9 | |
| α-helix | 290-293 | 4 | |
| β-strand | 296-297 | 2 | 8 |
| β-strand | 300-309 | 10 | 9 |
| α-helix | 319-328 | 10 | |
| α-helix | 331-337 | 7 | |
| β-strand | 346-347 | 2 | 9 |
| α-helix | 375-384 | 10 | |
| β-strand | 391-397 | 7 | 9 |
| α-helix | 401-414 | 14 | |
| β-strand | 418-424 | 7 | 9 |
| α-helix | 430-434 | 5 | |
| α-helix | 438-443 | 6 | |
| β-strand | 446-453 | 8 | 9 |
| α-helix | 460-468 | 9 | |
| α-helix | 470-472 | 3 | |
| α-helix | 488-498 | 11 | |
| α-helix | 503-520 | 18 | |
| β-strand | 523-530 | 8 | 9 |
| β-strand | 533-534 | 2 | 8 |
| β-strand | 539-540 | 2 | 10 |
| β-strand | 542 | 1 | 1 |
| β-strand | 544 | 1 | 11 |
| β-strand | 551 | 1 | 11 |
| α-helix | 553-555 | 3 | |
| β-strand | 557-558 | 2 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Clavulanic acid biosynthesis oligopeptide binding protein 2 | A | protein | 562 | Streptomyces clavuligerus | Q8KRB4 (AlphaFold model) |
| Kininogen-1 | B | protein | 9 | Homo sapiens | P01042 (AlphaFold model) |
>2WOK_1 CLAVULANIC ACID BIOSYNTHESIS OLIGOPEPTIDE BINDING PROTEIN 2 (chains A) MTTAARRPAPTTAGAGWDAGVGALVNPSRRRGGTLRLVSSADVDSLDPARTYYVWVWLLQ RLLNRTLMAYPTDPGPAGLVPAPDLAEGPGEVSDGGRTWTYRLRRGLRYDDGTPITSDDV RHAVQRVFAQDVLPGGPTYLIPLLDDPERPYPGPYRTDEPLRSVLTPDEHTIVFRLTRPF SDFDHLMAQPCAAPVPRRSDTGADYGRDPRSSGPYRVARHEPDTLLHLERNPHWDRATDP IRPALPDRVELTIGLDVDVLDARLIAGEFDINLEGRGLQHAAQRRATADEVLRSHTDNPR TSFLHFVAMQPHIPPFDNVHVRRAVQYAADKILLQDARGGPVNGGDLTTALFPPTLPAHQ DLDLYPTGPDLRGDLDAARAELAAAGLPDGFRAVIGTQRGKFRLVADAVVESLARVGIEL TVKELDVATYFSLGAGHPETVREHGLGLLVTDWGADFPTEYGFLAPLVDGRQIKRNGGNW NLPELDDPEVNALIDETLHTTDPAARAELWRAVERRVMEHAVLLPLVHDKTLHFRNPWVT NVYVHPAFGLYDIQAMGLAEED
>2WOK_2 Kininogen-1 (chains B) RPPGFSPFR
Crystal structures of an oligopeptide-binding protein from the biosynthetic pathway of the beta-lactamase inhibitor clavulanic acid. Mackenzie, A.K., Valegard, K., Iqbal, A. et al. J Mol Biol (2010) 396:332-344. DOI 10.1016/j.jmb.2009.11.045 · PubMed
Other PDB entries of the same protein (UniProt Q8KRB4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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