Complex (antibody/antigen). Determined by X-ray diffraction at 2.8 Å resolution. Released 25 Mar 1998.
Explore 1JRH in 3D Show helices and sheets RCSB PDB PDBe
1JRH contains 11 α-helices and 52 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 | 3-7 | 5 | 7 |
| β-strand | 11-12 | 2 | 8 |
| β-strand | 18-25 | 8 | 7 |
| β-strand | 35-39 | 7 | 9 |
| β-strand | 46-52 | 7 | 9 |
| β-strand | 57-59 | 3 | 9 |
| α-helix | 64-66 | 3 | |
| β-strand | 67-72 | 6 | 7 |
| β-strand | 77-82 | 6 | 7 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 9 |
| α-helix | 96 | 1 | |
| β-strand | 100D-103 | 4 | 9 |
| β-strand | 107-109 | 3 | 9 |
| β-strand | 110-111 | 2 | 8 |
| β-strand | 143 | 1 | 10 |
| β-strand | 153-156 | 3 | 11 |
| β-strand | 171-173 | 3 | 12 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 13 |
| β-strand | 185-186 | 2 | 13 |
| β-strand | 188 | 1 | 10 |
| β-strand | 189-191 | 3 | 12 |
| β-strand | 209-212 | 4 | 11 |
| α-helix | 213-215 | 3 | |
| β-strand | 217-219 | 3 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-15 | 4 | |
| β-strand | 16-21 | 6 | 14 |
| β-strand | 28-32 | 5 | 14 |
| β-strand | 41-49 | 9 | 15 |
| β-strand | 53 | 1 | 15 |
| β-strand | 57-63 | 7 | 15 |
| β-strand | 67-69 | 3 | 14 |
| α-helix | 71-73 | 3 | |
| β-strand | 80-89 | 10 | 15 |
| β-strand | 92-93 | 2 | 15 |
| α-helix | 94-96 | 3 | |
| β-strand | 97-98 | 2 | 15 |
| β-strand | 102 | 1 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 2 |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 3 |
| β-strand | 114-116 | 3 | 4 |
| β-strand | 135-139 | 5 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-146 | 2 | 5 |
| β-strand | 162-163 | 2 | 4 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-176 | 4 | 4 |
| β-strand | 195 | 1 | 6 |
| β-strand | 196-197 | 2 | 5 |
| β-strand | 206 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Antibody A6 | L | protein | 213 | Mus musculus | P01837 (AlphaFold model) |
| Antibody A6 | H | protein | 219 | Mus musculus | P01869 (AlphaFold model) |
| Interferon-gamma receptor alpha chain | I | protein | 108 | Homo sapiens | P15260 (AlphaFold model) |
>1JRH_1 ANTIBODY A6 (chains L) SVEMTQSPSSFSVSLGDRVTITCKASEDIYNRLAWYQQKPGNAPRLLISGATSLETEVPS RFSGSGSGKDYTLSITSLQTEDVATYYCQQYWSTWTFGGGTKLEIKRADAAPTVSIFPPS SEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTL TKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1JRH_2 ANTIBODY A6 (chains H) AVKLQESGPGILKPSQTLSLTCSFSGFSLTTYGMGVGWIRQSSGKGLEWLAHIWWDDDKY YNPSLKSRLTISKDTSRNQVFLKITSVATADTATYYCARRAPFYGNHAMDYWGQGTTVTV SSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQ SDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKI
>1JRH_3 INTERFERON-GAMMA RECEPTOR ALPHA CHAIN (chains I) EMGTADLGPSSVPTPTNVTIESYNMNPIVYWEYQIMPQVPVFTVEVKNYGVKNSEWIDAC INISHHYCNISDHVGDPSNSLWVRVKARVGQKESAYAKSEEFAVSRDG
Neutralizing epitopes on the extracellular interferon gamma receptor (IFNgammaR) alpha-chain characterized by homolog scanning mutagenesis and X-ray crystal structure of the A6 fab-IFNgammaR1-108 complex. Sogabe, S., Stuart, F., Henke, C. et al. J Mol Biol (1997) 273:882-897. DOI 10.1006/jmbi.1997.1336 · PubMed
Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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