Human FcRn extra-cellular domain complexed with Fab fragment of Rozanolixizumab. Determined by X-ray diffraction at 2.9 Å resolution. Released 29 Aug 2018.
Explore 6FGB in 3D Show helices and sheets RCSB PDB PDBe
6FGB contains 25 α-helices and 74 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 | 49-53 | 5 | |
| α-helix | 60-81 | 22 | |
| 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 | 159-169 | 11 | |
| α-helix | 171-175 | 5 | |
| 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 |
| β-strand | 250-256 | 7 | 4 |
| β-strand | 263-266 | 4 | 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 | 36-41 | 6 | 7 |
| β-strand | 44-45 | 2 | 7 |
| β-strand | 50-51 | 2 | 6 |
| β-strand | 55-56 | 2 | 6 |
| β-strand | 62-70 | 9 | 6 |
| β-strand | 78-83 | 6 | 7 |
| β-strand | 91-94 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-7 | 2 | 15 |
| β-strand | 10-12 | 3 | 16 |
| β-strand | 18-23 | 6 | 15 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 16 |
| β-strand | 46-51 | 6 | 16 |
| β-strand | 58-60 | 3 | 16 |
| β-strand | 68-73 | 6 | 15 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 15 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 16 |
| β-strand | 111-115 | 5 | 16 |
| α-helix | 119-120 | 2 | |
| β-strand | 121 | 1 | 17 |
| α-helix | 122-123 | 2 | |
| β-strand | 124-128 | 5 | 18 |
| α-helix | 129-131 | 3 | |
| β-strand | 139-149 | 11 | 18 |
| β-strand | 150 | 1 | 17 |
| β-strand | 155-158 | 4 | 19 |
| α-helix | 159-161 | 3 | |
| β-strand | 167-169 | 3 | 18 |
| α-helix | 170-172 | 3 | |
| β-strand | 173-175 | 3 | 18 |
| β-strand | 179-189 | 11 | 18 |
| α-helix | 192-195 | 4 | |
| β-strand | 196 | 1 | 20 |
| β-strand | 199-204 | 6 | 19 |
| β-strand | 209-214 | 6 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 8 |
| β-strand | 10-14 | 5 | 9 |
| β-strand | 19-25 | 7 | 8 |
| β-strand | 30 | 1 | 10 |
| β-strand | 36 | 1 | 10 |
| β-strand | 38-43 | 6 | 9 |
| β-strand | 50-54 | 5 | 9 |
| β-strand | 58-59 | 2 | 9 |
| α-helix | 60 | 1 | |
| β-strand | 67-71 | 5 | 8 |
| β-strand | 75-80 | 6 | 8 |
| α-helix | 85-87 | 3 | |
| β-strand | 89-95 | 7 | 9 |
| β-strand | 102-103 | 2 | 9 |
| β-strand | 107-112 | 6 | 9 |
| β-strand | 116 | 1 | 11 |
| β-strand | 119-123 | 5 | 12 |
| α-helix | 124-126 | 3 | |
| α-helix | 127-131 | 5 | |
| β-strand | 134-144 | 11 | 12 |
| β-strand | 145 | 1 | 11 |
| β-strand | 149-153 | 5 | 13 |
| β-strand | 154-155 | 2 | 14 |
| β-strand | 158-159 | 2 | 14 |
| β-strand | 164-168 | 5 | 12 |
| α-helix | 169-172 | 4 | |
| β-strand | 178-187 | 10 | 12 |
| α-helix | 188-193 | 6 | |
| β-strand | 196-203 | 8 | 13 |
| β-strand | 210-215 | 6 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IgG receptor FcRn large subunit p51 | A | protein | 342 | Homo sapiens | P55899 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 99 | Homo sapiens | P61769 (AlphaFold model) |
| 1519.g57- Light chain | L | protein | 219 | Homo sapiens | |
| 1519.g57- Heavy chain | H | protein | 228 | Homo sapiens |
>6FGB_1 IgG receptor FcRn large subunit p51 (chains A) AESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWY WEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNF DLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPP SMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSL TVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSSVLVVGIVIGVLLLTAAAVGGALLWRR MRSGLPAPWISLRGDDTGVLLPTPGEAQDADLKDVNVIPATA
>6FGB_2 Beta-2-microglobulin (chains B) IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>6FGB_3 1519.g57- Light chain (chains L) DIQMTQSPSSLSASVGDRVTITCKSSQSLVGASGKTYLYWLFQKPGKAPKRLIYLVSTLD SGIPSRFSGSGSGTEFTLTISSLQPEDFATYYCLQGTHFPHTFGQGTKLEIKRTVAAPSV FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>6FGB_4 1519.g57- Heavy chain (chains H) EVPLVESGGGLVQPGGSLRLSCAVSGFTFSNYGMVWVRQAPGKGLEWVAYIDSDGDNTYY RDSVKGRFTISRDNAKSSLYLQMNSLRAEDTAVYYCTTGIVRPFLYWGQGTLVTVSSAST KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY SLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCAA
Generation and characterization of a high affinity anti-human FcRn antibody, rozanolixizumab, and the effects of different molecular formats on the reduction of plasma IgG concentration. Smith, B., Kiessling, A., Lledo-Garcia, R. et al. MAbs (2018) 10:1111-1130. DOI 10.1080/19420862.2018.1505464 · 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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