Crystal structure of the Neisseria meningitidis Factor H binding protein, fHbp (GNA1870) at 2.0 A resolution. Determined by X-ray diffraction at 2.0 Å resolution. Released 29 Dec 2010.
Explore 3KVD in 3D Show helices and sheets RCSB PDB PDBe
3KVD contains 7 α-helices and 19 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 | 81-86 | 6 | |
| α-helix | 88-89 | 2 | |
| β-strand | 99-100 | 2 | 1 |
| β-strand | 110-115 | 6 | 2 |
| β-strand | 118-122 | 5 | 2 |
| β-strand | 127-128 | 2 | 1 |
| α-helix | 130-132 | 3 | |
| α-helix | 134 | 1 | |
| β-strand | 138-149 | 12 | 2 |
| β-strand | 152-165 | 14 | 2 |
| β-strand | 169-180 | 12 | 2 |
| β-strand | 188-201 | 14 | 2 |
| β-strand | 203 | 1 | 3 |
| α-helix | 204 | 1 | |
| β-strand | 205 | 1 | 4 |
| α-helix | 206-208 | 3 | |
| β-strand | 214-223 | 10 | 3 |
| β-strand | 226-236 | 11 | 3 |
| β-strand | 241-247 | 7 | 3 |
| α-helix | 252-254 | 3 | |
| β-strand | 257-265 | 9 | 3 |
| β-strand | 270 | 1 | 4 |
| β-strand | 271-279 | 9 | 3 |
| β-strand | 282-292 | 11 | 3 |
| β-strand | 298-307 | 10 | 3 |
| β-strand | 310-319 | 10 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lipoprotein | D | protein | 242 | Neisseria meningitidis | Q6QCC2 (AlphaFold model) |
>3KVD_1 Lipoprotein (chains D) AGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTGKLKNDKV SRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAKRQFRIGD IAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKSPELNVDL AAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGGKAQEVAGSAEVKTVNGIRHIGLAA KQ
Structure of the uncomplexed Neisseria meningitidis factor H-binding protein fHbp (rLP2086). Cendron, L., Veggi, D., Girardi, E. et al. Acta Crystallogr Sect F Struct Biol Cryst Commun (2011) 67:531-535. DOI 10.1107/S1744309111006154 · PubMed
Other PDB entries of the same protein (UniProt Q6QCC2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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