Neonatal fc receptor, PH 6.5. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Jun 1998.
Explore 3FRU in 3D Show helices and sheets RCSB PDB PDBe
3FRU contains 33 α-helices and 87 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 | 7-14 | 8 | 1 |
| 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 | 60-85 | 26 | |
| β-strand | 91-100 | 10 | 1 |
| β-strand | 106-114 | 9 | 1 |
| β-strand | 117-123 | 7 | 1 |
| β-strand | 128-130 | 3 | 1 |
| α-helix | 134-143 | 10 | |
| α-helix | 147-155 | 9 | |
| α-helix | 156-160 | 5 | |
| α-helix | 161-171 | 11 | |
| α-helix | 173-176 | 4 | |
| β-strand | 180 | 1 | 2 |
| α-helix | 181-182 | 2 | |
| β-strand | 183-190 | 8 | 3 |
| β-strand | 195-205 | 11 | 3 |
| β-strand | 206 | 1 | 2 |
| β-strand | 211-216 | 6 | 4 |
| β-strand | 219-220 | 2 | 4 |
| β-strand | 225-230 | 6 | 3 |
| β-strand | 236-245 | 10 | 3 |
| α-helix | 249-251 | 3 | |
| β-strand | 252-257 | 6 | 4 |
| β-strand | 265-267 | 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 | 7-14 | 8 | 8 |
| 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 | 60-85 | 26 | |
| β-strand | 91-100 | 10 | 8 |
| β-strand | 106-114 | 9 | 8 |
| β-strand | 117-123 | 7 | 8 |
| β-strand | 128-130 | 3 | 8 |
| α-helix | 134-143 | 10 | |
| α-helix | 148-155 | 8 | |
| α-helix | 156-160 | 5 | |
| α-helix | 161-171 | 11 | |
| α-helix | 173-177 | 5 | |
| β-strand | 180 | 1 | 9 |
| α-helix | 181-182 | 2 | |
| β-strand | 183-190 | 8 | 10 |
| β-strand | 195-205 | 11 | 10 |
| β-strand | 206 | 1 | 9 |
| β-strand | 211-216 | 6 | 11 |
| β-strand | 219-220 | 2 | 11 |
| β-strand | 225-230 | 6 | 10 |
| β-strand | 236-245 | 10 | 10 |
| α-helix | 249-251 | 3 | |
| β-strand | 252-257 | 6 | 11 |
| β-strand | 265-267 | 3 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-14 | 8 | 15 |
| β-strand | 24-30 | 7 | 15 |
| β-strand | 33-39 | 7 | 15 |
| β-strand | 46-47 | 2 | 15 |
| α-helix | 49-52 | 4 | |
| α-helix | 60-85 | 26 | |
| β-strand | 91-100 | 10 | 15 |
| β-strand | 106-114 | 9 | 15 |
| β-strand | 117-123 | 7 | 15 |
| β-strand | 128-130 | 3 | 15 |
| α-helix | 134-143 | 10 | |
| α-helix | 147-155 | 9 | |
| α-helix | 156-160 | 5 | |
| α-helix | 161-171 | 11 | |
| α-helix | 173-176 | 4 | |
| β-strand | 180 | 1 | 16 |
| α-helix | 181-182 | 2 | |
| β-strand | 183-190 | 8 | 17 |
| β-strand | 195-205 | 11 | 17 |
| β-strand | 206 | 1 | 16 |
| β-strand | 211-216 | 6 | 18 |
| β-strand | 219-220 | 2 | 18 |
| β-strand | 225-230 | 6 | 17 |
| β-strand | 236-245 | 10 | 17 |
| α-helix | 249-251 | 3 | |
| β-strand | 252-257 | 6 | 18 |
| β-strand | 265-267 | 3 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neonatal fc receptor | A, C, E | protein | 269 | Rattus norvegicus | P13599 (AlphaFold model) |
| Beta-2-microglobulin | B, D, F | protein | 99 | Rattus norvegicus | P07151 (AlphaFold model) |
>3FRU_1 NEONATAL FC RECEPTOR (chains A, C, E) AEPRLPLMYHLAAVSDLSTGLPSFWATGWLGAQQYLTYNNLRQEADPCGAWIWENQVSWY WEKETTDLKSKEQLFLEAIRTLENQINGTFTLQGLLGCELAPDNSSLPTAVFALNGEEFM RFNPRTGNWSGEWPETDIVGNLWMKQPEAARKESEFLLTSCPERLLGHLERGRQNLEWKE PPSMRLKARPGNSGSSVLTCAAFSFYPPELKFRFLRNGLASGSGNCSTGPNGDGSFHAWS LLEVKRGDEHHYQCQVEHEGLAQPLTVDL
>3FRU_2 BETA-2-MICROGLOBULIN (chains B, D, F) IQKTPQIQVYSRHPPENGKPNFLNCYVSQFHPPQIEIELLKNGKKIPNIEMSDLSFSKDW SFYILAHTEFTPTETDVYACRVKHVTLKEPKTVTWDRDM
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Water and common crystallization additives (BME, SO4) are not listed.
Structural basis of pH-dependent antibody binding by the neonatal Fc receptor. Vaughn, D.E., Bjorkman, P.J. Structure (1998) 6:63-73. DOI 10.1016/S0969-2126(98)00008-2 · PubMed
Other PDB entries of the same protein (UniProt P13599 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3FRU directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.