Crystal structure of SYNT001, a human FcRn blocking monoclonal antibody. Determined by X-ray diffraction at 2.38 Å resolution. Released 25 Dec 2019.
Explore 6NHA in 3D Show helices and sheets RCSB PDB PDBe
6NHA contains 27 α-helices and 69 β-strands across 4 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 | 6-14 | 9 | 1 |
| α-helix | 17-18 | 2 | |
| β-strand | 24-30 | 7 | 1 |
| β-strand | 33-39 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 49-52 | 4 | |
| α-helix | 59-78 | 20 | |
| α-helix | 79-81 | 3 | |
| β-strand | 89-98 | 10 | 1 |
| β-strand | 104-112 | 9 | 1 |
| β-strand | 115-121 | 7 | 1 |
| β-strand | 126-128 | 3 | 1 |
| α-helix | 132-142 | 11 | |
| α-helix | 147-153 | 7 | |
| α-helix | 154-158 | 5 | |
| α-helix | 159-165 | 7 | |
| β-strand | 178 | 1 | 2 |
| α-helix | 179-180 | 2 | |
| β-strand | 181-188 | 8 | 3 |
| β-strand | 193-203 | 11 | 3 |
| β-strand | 204 | 1 | 2 |
| β-strand | 208-214 | 7 | 4 |
| β-strand | 217-218 | 2 | 4 |
| β-strand | 223-228 | 6 | 3 |
| β-strand | 234-243 | 10 | 3 |
| α-helix | 246-249 | 4 | |
| β-strand | 250-256 | 7 | 4 |
| β-strand | 263-265 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 6 |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 35-41 | 7 | 7 |
| β-strand | 44-45 | 2 | 7 |
| β-strand | 50-51 | 2 | 6 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 6 |
| β-strand | 62-70 | 9 | 6 |
| β-strand | 78-84 | 7 | 7 |
| β-strand | 91-94 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 13 |
| β-strand | 10-12 | 3 | 9 |
| β-strand | 18-25 | 8 | 13 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 9 |
| β-strand | 46-51 | 6 | 9 |
| β-strand | 58-60 | 3 | 9 |
| β-strand | 68-73 | 6 | 13 |
| β-strand | 78-83 | 6 | 13 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 9 |
| β-strand | 108 | 1 | 9 |
| β-strand | 112-116 | 5 | 9 |
| α-helix | 119-121 | 3 | |
| α-helix | 123-124 | 2 | |
| β-strand | 125-129 | 5 | 14 |
| β-strand | 140-150 | 11 | 14 |
| β-strand | 156-159 | 4 | 15 |
| α-helix | 160-162 | 3 | |
| β-strand | 168-170 | 3 | 14 |
| α-helix | 171-173 | 3 | |
| β-strand | 174-175 | 2 | 14 |
| β-strand | 181-190 | 10 | 14 |
| α-helix | 191-194 | 4 | |
| β-strand | 200-205 | 6 | 15 |
| β-strand | 210-215 | 6 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 8 |
| β-strand | 10-13 | 4 | 9 |
| β-strand | 19-25 | 7 | 8 |
| β-strand | 33-38 | 6 | 9 |
| β-strand | 45-49 | 5 | 9 |
| β-strand | 53-54 | 2 | 9 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 8 |
| β-strand | 70-75 | 6 | 8 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 9 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 9 |
| β-strand | 102-106 | 5 | 9 |
| β-strand | 111 | 1 | 10 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 11 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 11 |
| β-strand | 140 | 1 | 10 |
| β-strand | 145-150 | 6 | 12 |
| β-strand | 153-154 | 2 | 12 |
| β-strand | 159-163 | 5 | 11 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-182 | 10 | 11 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 12 |
| β-strand | 205-210 | 6 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IgG receptor FcRn large subunit p51 | A | protein | 279 | Homo sapiens | P55899 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 99 | Homo sapiens | P61769 (AlphaFold model) |
| SYNT001-Fab light chain | L | protein | 214 | Homo sapiens | |
| SYNT001-Fab heavy chain | H | protein | 220 | Homo sapiens |
>6NHA_1 IgG receptor FcRn large subunit p51 (chains A) AESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWY WEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDATSVPTAKFALNGEEFMNF DLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPP SMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSL TVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSENLYFQ
>6NHA_2 Beta-2-microglobulin (chains B) IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>6NHA_3 SYNT001-Fab light chain (chains L) DIQMTQSPSSLSASVGDRVTITCKASDHINNWLAWYQQKPGQAPRLLISGATSLETGVPS RFSGSGTGKDYTLTISSLQPEDFATYYCQQYWSTPYTFGGGTKVEIKRTVAAPSVFIFPP SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>6NHA_4 SYNT001-Fab heavy chain (chains H) QVQLVQSGAELKKPGASVKLSCKASGYTFTSYGISWVKQATGQGLEWIGEIYPRSGNTYY NEKFKGRATLTADKSTSTAYMELRSLRSEDSAVYFCARSTTVRPPGIWGTGTTVTVSSAS TKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGL YSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESKY
| ID | Name | Formula | Copies |
|---|---|---|---|
| NHE | 2-[N-cyclohexylamino]ethane sulfonic acid | C8 H17 N O3 S | 3 |
Blocking FcRn in humans reduces circulating IgG levels and inhibits IgG immune complex-mediated immune responses. Blumberg, L.J., Humphries, J.E., Jones, S.D. et al. Sci Adv (2019) 5:eaax9586-eaax9586. DOI 10.1126/sciadv.aax9586 · PubMed
Other PDB entries of the same protein (UniProt P55899 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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