Structure of a complex between CCPs 6 and 7 of Human Complement Factor H and Neisseria meningitidis FHbp Variant 3 P106A mutant. Determined by X-ray diffraction at 3.0 Å resolution. Released 7 Nov 2012.
Explore 4AYM in 3D Show helices and sheets RCSB PDB PDBe
4AYM contains 35 α-helices and 90 β-strands across 6 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 |
|---|---|---|---|
| β-strand | 333-335 | 3 | 1 |
| α-helix | 338-341 | 4 | |
| α-helix | 342-344 | 3 | |
| β-strand | 352-357 | 6 | 1 |
| β-strand | 361-362 | 2 | 2 |
| β-strand | 369-375 | 7 | 1 |
| β-strand | 378-380 | 3 | 1 |
| β-strand | 386-387 | 2 | 2 |
| β-strand | 388-390 | 3 | 3 |
| α-helix | 391-393 | 3 | |
| β-strand | 397 | 1 | 4 |
| β-strand | 405-407 | 3 | 3 |
| β-strand | 411-413 | 3 | 5 |
| β-strand | 416 | 1 | 4 |
| α-helix | 417 | 1 | |
| α-helix | 423-425 | 3 | |
| β-strand | 428-432 | 5 | 5 |
| β-strand | 435-437 | 3 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 88-89 | 2 | |
| β-strand | 99 | 1 | 11 |
| α-helix | 102-104 | 3 | |
| β-strand | 110-115 | 6 | 12 |
| β-strand | 118-123 | 6 | 12 |
| β-strand | 128 | 1 | 11 |
| α-helix | 130-132 | 3 | |
| α-helix | 134 | 1 | |
| β-strand | 138-147 | 10 | 12 |
| β-strand | 154-165 | 12 | 12 |
| β-strand | 169-180 | 12 | 12 |
| β-strand | 188-201 | 14 | 12 |
| β-strand | 203 | 1 | 13 |
| α-helix | 204 | 1 | |
| β-strand | 205 | 1 | 14 |
| α-helix | 206-208 | 3 | |
| β-strand | 214-223 | 10 | 13 |
| β-strand | 226-236 | 11 | 13 |
| β-strand | 241-247 | 7 | 13 |
| α-helix | 255 | 1 | |
| β-strand | 256-265 | 10 | 13 |
| β-strand | 270 | 1 | 14 |
| β-strand | 271-279 | 9 | 13 |
| β-strand | 282-292 | 11 | 13 |
| β-strand | 298-307 | 10 | 13 |
| β-strand | 310-319 | 10 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 82-86 | 5 | |
| α-helix | 88-89 | 2 | |
| β-strand | 99-100 | 2 | 15 |
| α-helix | 102-104 | 3 | |
| β-strand | 110-115 | 6 | 16 |
| β-strand | 118-123 | 6 | 16 |
| β-strand | 127-128 | 2 | 15 |
| α-helix | 130-132 | 3 | |
| α-helix | 134 | 1 | |
| β-strand | 138-149 | 12 | 16 |
| β-strand | 152-165 | 14 | 16 |
| β-strand | 169-180 | 12 | 16 |
| β-strand | 188-201 | 14 | 16 |
| β-strand | 203 | 1 | 17 |
| α-helix | 204 | 1 | |
| β-strand | 205 | 1 | 18 |
| α-helix | 206-208 | 3 | |
| β-strand | 214-223 | 10 | 17 |
| β-strand | 226-236 | 11 | 17 |
| β-strand | 241-247 | 7 | 17 |
| α-helix | 255 | 1 | |
| β-strand | 256-265 | 10 | 17 |
| β-strand | 270 | 1 | 18 |
| β-strand | 271-278 | 8 | 17 |
| β-strand | 285-292 | 8 | 17 |
| β-strand | 298-307 | 10 | 17 |
| β-strand | 310-319 | 10 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement factor H | A, B, E, F | protein | 125 | HOMO SAPIENS | P08603 (AlphaFold model) |
| Factor H binding protein | C, D | protein | 270 | NEISSERIA MENINGITIDIS MC58 | Q19KF7 (AlphaFold model) |
>4AYM_1 COMPLEMENT FACTOR H (chains A, B, E, F) MGTLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDG WSPAVPCLRKCYFPYLENGYNQNHGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSP TPRCI
>4AYM_2 FACTOR H BINDING PROTEIN (chains C, D) MGPDSDRLQQRRVAADIGTGLADALTAPLDHKDKGLKSLTLEDSIAQNGTLTLSAQGAEK TFKAGDKDNSLNTGKLKNDKISRFDFVQKIEVDGQTITLASGEFQIYKQNHSAVVALQIE KINNPDKTDSLINQRSFLVSGLGGEHTAFNQLPGGKAEYHGKAFSSDDPNGRLHYSIDFT KKQGYGRIEHLKTLEQNVELAAAELKADEKSHAVILGDTRYGSEEKGTYHLALFGDRAQE IAGSATVKIGEKVHEIGIAGKQLEHHHHHH
Design and Evaluation of Meningococcal Vaccines Through Structure-Based Modification of Host and Pathogen Molecules. Johnson, S., Tan, L., Van Der Veen, S. et al. PLoS Pathog (2012) 8:2981. DOI 10.1371/JOURNAL.PPAT.1002981 · PubMed
Other PDB entries of the same protein (UniProt P08603 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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