Crystal structure of the neonatal fc receptor complexed with a heterodimeric fc. Determined by X-ray diffraction at 2.8 Å resolution. Released 14 Feb 2001.
Explore 1I1A in 3D Show helices and sheets RCSB PDB PDBe
1I1A contains 25 α-helices and 66 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 | 7-14 | 8 | 1 |
| β-strand | 24-30 | 7 | 1 |
| β-strand | 33-39 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 49-51 | 3 | |
| 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 | 134-144 | 11 | |
| α-helix | 147-155 | 9 | |
| α-helix | 156-160 | 5 | |
| α-helix | 161-176 | 16 | |
| β-strand | 183-189 | 7 | 2 |
| β-strand | 195-205 | 11 | 2 |
| β-strand | 211-216 | 6 | 3 |
| β-strand | 219-220 | 2 | 3 |
| β-strand | 226-230 | 5 | 2 |
| β-strand | 236-245 | 10 | 2 |
| α-helix | 249-251 | 3 | |
| β-strand | 252-257 | 6 | 3 |
| β-strand | 265-267 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 4 |
| β-strand | 6-11 | 6 | 5 |
| β-strand | 21-30 | 10 | 5 |
| β-strand | 31 | 1 | 4 |
| β-strand | 36-41 | 6 | 6 |
| β-strand | 44-45 | 2 | 6 |
| β-strand | 50-51 | 2 | 5 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 5 |
| β-strand | 62-70 | 9 | 5 |
| β-strand | 78-83 | 6 | 6 |
| β-strand | 91-94 | 4 | 6 |
| α-helix | 95 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 240-243 | 4 | 7 |
| α-helix | 244-246 | 3 | |
| α-helix | 247-251 | 5 | |
| β-strand | 258-263 | 6 | 7 |
| β-strand | 274-279 | 6 | 8 |
| β-strand | 283-284 | 2 | 8 |
| β-strand | 288-294 | 7 | 7 |
| β-strand | 300-307 | 8 | 7 |
| α-helix | 310-314 | 5 | |
| β-strand | 319-324 | 6 | 8 |
| β-strand | 332-336 | 5 | 8 |
| α-helix | 338-340 | 3 | |
| β-strand | 344 | 1 | 9 |
| β-strand | 347-351 | 5 | 10 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-357 | 3 | |
| β-strand | 362-372 | 11 | 10 |
| β-strand | 373 | 1 | 9 |
| β-strand | 378-383 | 6 | 11 |
| β-strand | 386-387 | 2 | 11 |
| β-strand | 391-393 | 3 | 10 |
| α-helix | 394-396 | 3 | |
| β-strand | 397-398 | 2 | 10 |
| β-strand | 404-413 | 10 | 10 |
| α-helix | 414-418 | 5 | |
| β-strand | 423-428 | 6 | 11 |
| α-helix | 433-435 | 3 | |
| β-strand | 436-441 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 247-250 | 4 | |
| α-helix | 256-257 | 2 | |
| β-strand | 258-259 | 2 | 12 |
| β-strand | 276-278 | 3 | 13 |
| β-strand | 283 | 1 | 13 |
| β-strand | 288-290 | 3 | 14 |
| β-strand | 295 | 1 | 15 |
| β-strand | 299 | 1 | 15 |
| β-strand | 303-305 | 3 | 14 |
| β-strand | 306-307 | 2 | 12 |
| α-helix | 310-313 | 4 | |
| β-strand | 320-322 | 3 | 13 |
| β-strand | 344 | 1 | 16 |
| β-strand | 347-351 | 5 | 17 |
| α-helix | 352-354 | 3 | |
| β-strand | 362-372 | 11 | 17 |
| β-strand | 373 | 1 | 16 |
| β-strand | 379-383 | 5 | 18 |
| β-strand | 386-387 | 2 | 18 |
| β-strand | 391-393 | 3 | 17 |
| α-helix | 394-396 | 3 | |
| β-strand | 397-398 | 2 | 17 |
| β-strand | 404-413 | 10 | 17 |
| α-helix | 414-418 | 5 | |
| β-strand | 423-428 | 6 | 18 |
| α-helix | 433-435 | 3 | |
| β-strand | 436-441 | 6 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neonatal fc receptor A | A | protein | 269 | Rattus norvegicus | P13599 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 99 | Rattus norvegicus | P07151 (AlphaFold model) |
| Ig gamma-2A chain C region | C | protein | 225 | Rattus norvegicus | P20760 (AlphaFold model) |
| Ig gamma-2A chain C region | D | protein | 239 | Rattus norvegicus | P20760 (AlphaFold model) |
>1I1A_1 NEONATAL FC RECEPTOR A (chains A) AEPRLPLMYHLAAVSDLSTGLPSFWATGWLGAQQYLTYNNLRQEADPCGAWIWENQVSWY WEKETTDLKSKEQLFLEAIRTLENQINGTFTLQGLLGCELAPDNSSLPTAVFALNGEEFM RFNPRTGNWSGEWPETDIVGNLWMKQPEAARKESEFLLTSCPERLLGHLERGRQNLEWKE PPSMRLKARPGNSGSSVLTCAAFSFYPPELKFRFLRNGLASGSGNCSTGPNGDGSFHAWS LLEVKRGDEHHYQCQVEHEGLAQPLTVDL
>1I1A_2 BETA-2-MICROGLOBULIN (chains B) IQKTPQIQVYSRHPPENGKPNFLNCYVSQFHPPQIEIELLKNGKKIPNIEMSDLSFSKDW SFYILAHTEFTPTETDVYACRVKHVTLKEPKTVTWDRDM
>1I1A_3 IG GAMMA-2A CHAIN C REGION (chains C) VPRECNPCGCTGSEVSSVFIFPPKTKDVLTITLTPKVTCVVVDISQNDPEVRFSWFIDDV EVHTAQTHAPEKQSNSTLRSVSELPIVHRDWLNGKTFKCKVNSGAFPAPIEKSISKPEGT PRGPQVYTMAPPKEEMTQSQVSITCMVKGFYPPDIYTEWKMNGQPQENYKNTPPTMDTDG SYFLYSKLNVKKETWQQGNTFTCSVLHEGLHNHHTEKSLSHSPGK
>1I1A_4 IG GAMMA-2A CHAIN C REGION (chains D) VPRECNPCGCTGSEVSSVFIFPPKTKDVLGGGLTPKVTCVVVDISQNDPEVRFSWFIDDV EVHTAQTHAPEKQSNSTLRSVSELPIVERDWLNGKTFKCKVNSGAFPAPIEKSISKPEGT PRGPQVYTMAPPKEEMTQSQVSITCMVKGFYPPDIYTEWKMNGQPQENYKNTPPTMDTDG SYFLYSKLNVKKETWQQGNTFTCSVLHEGLENEHTEKSLSHSPGKGIEGRGSSHHHHHH
Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding. Martin, W.L., West Jr., A.P., Gan, L. et al. Mol Cell (2001) 7:867-877. DOI 10.1016/S1097-2765(01)00230-1 · PubMed
Other PDB entries of the same protein (UniProt P13599 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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