Crystal structure of FcRn at pH3. Determined by X-ray diffraction at 2.0 Å resolution. Released 30 May 2018.
Explore 6C97 in 3D Show helices and sheets RCSB PDB PDBe
6C97 contains 25 α-helices and 59 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 |
|---|---|---|---|
| α-helix | 5 | 1 | |
| 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 | 60-82 | 23 | |
| 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 | 171-174 | 4 | |
| 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 | 209-214 | 6 | 4 |
| β-strand | 217-220 | 4 | 4 |
| β-strand | 223-228 | 6 | 3 |
| β-strand | 234-243 | 10 | 3 |
| α-helix | 247-249 | 3 | |
| β-strand | 250-255 | 6 | 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 | 36-41 | 6 | 7 |
| β-strand | 44-45 | 2 | 7 |
| α-helix | 46 | 1 | |
| 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 | 6-14 | 9 | 8 |
| α-helix | 17-18 | 2 | |
| β-strand | 24-30 | 7 | 8 |
| β-strand | 33-39 | 7 | 8 |
| β-strand | 46-47 | 2 | 8 |
| α-helix | 49-53 | 5 | |
| α-helix | 60-82 | 23 | |
| β-strand | 89-98 | 10 | 8 |
| β-strand | 104-112 | 9 | 8 |
| β-strand | 115-121 | 7 | 8 |
| β-strand | 126-128 | 3 | 8 |
| α-helix | 132-142 | 11 | |
| α-helix | 147-153 | 7 | |
| α-helix | 154-158 | 5 | |
| α-helix | 159-169 | 11 | |
| α-helix | 171-174 | 4 | |
| β-strand | 178 | 1 | 9 |
| α-helix | 179-180 | 2 | |
| β-strand | 181-188 | 8 | 10 |
| β-strand | 193-203 | 11 | 10 |
| β-strand | 204 | 1 | 9 |
| β-strand | 209-214 | 6 | 11 |
| β-strand | 217-218 | 2 | 11 |
| β-strand | 223-228 | 6 | 10 |
| β-strand | 234-243 | 10 | 10 |
| α-helix | 247-249 | 3 | |
| β-strand | 250-255 | 6 | 11 |
| β-strand | 263-266 | 4 | 11 |
| β-strand | 267 | 1 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IgG receptor FcRn large subunit p51 | A, C | protein | 274 | Homo sapiens | P55899 (AlphaFold model) |
| Beta-2-microglobulin | B, D | protein | 99 | Homo sapiens | P61769 (AlphaFold model) |
>6C97_1 IgG receptor FcRn large subunit p51 (chains A, C) AESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWY WEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNF DLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPP SMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSL TVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSS
>6C97_2 Beta-2-microglobulin (chains B, D) IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Insight into small molecule binding to the neonatal Fc receptor by X-ray crystallography and 100 kHz magic-angle-spinning NMR. Stoppler, D., Macpherson, A., Smith-Penzel, S. et al. PLoS Biol (2018) 16:e2006192-e2006192. DOI 10.1371/journal.pbio.2006192 · 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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