Structure of a designed meningococcal antigen (factor H binding protein, mutant G1) inducing broad protective immunity. Determined by X-ray diffraction at 1.9 Å resolution. Released 27 Jul 2011.
Explore 2Y7S in 3D Show helices and sheets RCSB PDB PDBe
2Y7S contains 18 α-helices and 40 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 | 16-21 | 6 | |
| α-helix | 23-24 | 2 | |
| α-helix | 29 | 1 | |
| α-helix | 31 | 1 | |
| β-strand | 34-35 | 2 | 1 |
| β-strand | 45-50 | 6 | 2 |
| β-strand | 53-57 | 5 | 2 |
| α-helix | 61 | 1 | |
| β-strand | 62-63 | 2 | 1 |
| α-helix | 65-67 | 3 | |
| α-helix | 69 | 1 | |
| β-strand | 73-84 | 12 | 2 |
| β-strand | 87-100 | 14 | 2 |
| β-strand | 104-115 | 12 | 2 |
| β-strand | 123-136 | 14 | 2 |
| β-strand | 138 | 1 | 3 |
| α-helix | 139 | 1 | |
| β-strand | 140 | 1 | 4 |
| α-helix | 141-143 | 3 | |
| β-strand | 148-157 | 10 | 3 |
| β-strand | 160-170 | 11 | 3 |
| β-strand | 175-181 | 7 | 3 |
| α-helix | 186-188 | 3 | |
| β-strand | 191-199 | 9 | 3 |
| β-strand | 204 | 1 | 4 |
| β-strand | 205-213 | 9 | 3 |
| β-strand | 216-226 | 11 | 3 |
| β-strand | 232-239 | 8 | 3 |
| β-strand | 242 | 1 | 5 |
| β-strand | 244 | 1 | 5 |
| β-strand | 246-253 | 8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 16-21 | 6 | |
| α-helix | 23-24 | 2 | |
| α-helix | 29 | 1 | |
| β-strand | 34-35 | 2 | 6 |
| β-strand | 45-50 | 6 | 7 |
| β-strand | 53-57 | 5 | 7 |
| β-strand | 62-63 | 2 | 6 |
| α-helix | 65-67 | 3 | |
| α-helix | 69 | 1 | |
| β-strand | 73-84 | 12 | 7 |
| β-strand | 87-100 | 14 | 7 |
| β-strand | 104-116 | 13 | 7 |
| β-strand | 122-136 | 15 | 7 |
| β-strand | 138 | 1 | 8 |
| α-helix | 139 | 1 | |
| β-strand | 140 | 1 | 9 |
| α-helix | 141-143 | 3 | |
| β-strand | 148-157 | 10 | 8 |
| β-strand | 160-170 | 11 | 8 |
| β-strand | 175-181 | 7 | 8 |
| α-helix | 186-188 | 3 | |
| β-strand | 191-199 | 9 | 8 |
| β-strand | 204 | 1 | 9 |
| β-strand | 205-213 | 9 | 8 |
| β-strand | 216-226 | 11 | 8 |
| β-strand | 232-241 | 10 | 8 |
| β-strand | 244-253 | 10 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Factor H binding protein | A, B | protein | 256 | NEISSERIA MENINGITIDIS SEROGROUP B | Q9JXV4 (AlphaFold model) |
>2Y7S_1 FACTOR H BINDING PROTEIN (chains A, B) MVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTG KLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAK RQFRIGDLGGEHTAFNQLPDGKAEYRGTAFGSDDAGGKLTYTIDFTKKQGNGKIEHLKSP ELNVELASAEIKADGKSHAVILGDVRYGSEEKGSYSLGIFGGRAQEVAGSAEVKTVNGIR HIGLAAKQLEHHHHHH
Rational Design of a Meningococcal Antigen Inducing Broad Protective Immunity. Scarselli, M., Arico, B., Brunelli, B. et al. Sci Transl Med (2011) 3:91RA6. DOI 10.1126/SCITRANSLMED.3002234 · PubMed
Other PDB entries of the same protein (UniProt Q9JXV4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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