Crystal structure of a human type III fc gamma receptor in complex with an fc fragment of IgG1 (orthorhombic). Determined by X-ray diffraction at 3.0 Å resolution. Released 28 Sept 2004.
Explore 1T83 in 3D Show helices and sheets RCSB PDB PDBe
1T83 contains 17 α-helices and 61 β-strands across 3 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 | 239-243 | 5 | 1 |
| α-helix | 247-251 | 5 | |
| β-strand | 258-266 | 9 | 1 |
| β-strand | 274-279 | 6 | 2 |
| β-strand | 282-284 | 3 | 2 |
| β-strand | 288-289 | 2 | 1 |
| β-strand | 300-307 | 8 | 1 |
| α-helix | 310-315 | 6 | |
| β-strand | 321-324 | 4 | 2 |
| β-strand | 332-334 | 3 | 2 |
| α-helix | 338-340 | 3 | |
| β-strand | 344 | 1 | 3 |
| β-strand | 347-351 | 5 | 4 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-358 | 4 | |
| β-strand | 362-372 | 11 | 4 |
| β-strand | 373 | 1 | 3 |
| β-strand | 378-382 | 5 | 5 |
| β-strand | 387 | 1 | 5 |
| β-strand | 391-393 | 3 | 4 |
| α-helix | 394-396 | 3 | |
| β-strand | 397-398 | 2 | 4 |
| β-strand | 404-413 | 10 | 4 |
| α-helix | 414-419 | 6 | |
| β-strand | 423-428 | 6 | 5 |
| β-strand | 437-441 | 5 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 239-243 | 5 | 6 |
| α-helix | 247-251 | 5 | |
| β-strand | 258-266 | 9 | 6 |
| β-strand | 274 | 1 | 7 |
| β-strand | 277-279 | 3 | 8 |
| β-strand | 282-284 | 3 | 8 |
| β-strand | 287-290 | 4 | 6 |
| β-strand | 293-294 | 2 | 6 |
| β-strand | 299-307 | 9 | 6 |
| α-helix | 310-314 | 5 | |
| β-strand | 319-323 | 5 | 8 |
| β-strand | 324 | 1 | 7 |
| 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 | 378-382 | 5 | 11 |
| β-strand | 387 | 1 | 11 |
| β-strand | 391-393 | 3 | 10 |
| β-strand | 397-398 | 2 | 10 |
| β-strand | 404-413 | 10 | 10 |
| α-helix | 414-418 | 5 | |
| β-strand | 423-428 | 6 | 11 |
| β-strand | 437-441 | 5 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7 | 1 | 12 |
| β-strand | 9-13 | 5 | 13 |
| β-strand | 18-20 | 3 | 14 |
| β-strand | 25-30 | 6 | 13 |
| β-strand | 41-44 | 4 | 15 |
| β-strand | 47-49 | 3 | 15 |
| β-strand | 55-58 | 4 | 13 |
| α-helix | 63-65 | 3 | |
| β-strand | 67-68 | 2 | 16 |
| β-strand | 69-72 | 4 | 15 |
| β-strand | 77 | 1 | 12 |
| α-helix | 79-81 | 3 | |
| β-strand | 83-84 | 2 | 16 |
| β-strand | 85-87 | 3 | 14 |
| β-strand | 91-94 | 4 | 17 |
| β-strand | 106-112 | 7 | 17 |
| α-helix | 113-115 | 3 | |
| β-strand | 118-125 | 8 | 18 |
| β-strand | 129-135 | 7 | 18 |
| β-strand | 138-141 | 4 | 17 |
| β-strand | 150-158 | 9 | 18 |
| β-strand | 161-164 | 4 | 18 |
| α-helix | 166-167 | 2 | |
| β-strand | 168-170 | 3 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IGG1 | A, B | protein | 224 | Homo sapiens | P01857 (AlphaFold model) |
| Low affinity immunoglobulin gamma Fc region receptor III-B | C | protein | 176 | Homo sapiens | O75015 (AlphaFold model) |
>1T83_1 IGG1 (chains A, B) HTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVE VHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQP REPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGS FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
>1T83_2 Low affinity immunoglobulin gamma Fc region receptor III-B (chains C) RTEDLPKAVVFLEPQWYSVLEKDSVTLKCQGAYSPEDNSTQWFHNESLISSQASSYFIDA ATVNDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHK VTYLQNGKDRKYFHHNSDFHIPKATLKDSGSYFCRGLVGSKNVSSETVNITITQGL
| ID | Name | Formula | Copies |
|---|---|---|---|
| HG2 | Dibromomercury | Br2 Hg | 1 |
The structure of a human type III Fcgamma receptor in complex with Fc. Radaev, S., Motyka, S., Fridman, W.-H. et al. J Biol Chem (2001) 276:16469-16477. DOI 10.1074/jbc.M100350200 · PubMed
Other PDB entries of the same protein (UniProt P01857 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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