Research workbench
Interferon gamma signalling complex with IFNGR1 and IFNGR2
Analyse Interferon gamma signalling complex with IFNGR1 and IFNGR2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E3K
- Type
- protein
- Length
- 1,089 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01579, P15260, P38484
- Ligands
- NAG, MAN, BMA
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 125 | — | P01579 |
| B | — | protein | 126 | — | P01579 |
| C | — | protein | 207 | — | P15260 |
| D | — | protein | 203 | — | P15260 |
| E, I | — | protein | 214 | — | P38484 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 16 copies · chains B, E, A, I, C, D
- MAN · alpha-D-mannopyranose · sugar · 2 copies
- BMA · beta-D-mannopyranose · sugar
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B, C, D, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6E3K · Interferon gamma signalling complex with IFNGR1 and IFNGR2 · the same entry in another collection · chain A against A, TM-score 1.00
- P15260 · AlphaFold monomer V2.0 prediction for interferon gamma receptor 1 (P15260) · a predicted model of the same protein · chain D against A, TM-score 0.98
- P01579 · AlphaFold monomer V2.0 prediction for interferon gamma (P01579) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P38484 · AlphaFold monomer V2.0 prediction for interferon gamma receptor 2 (P38484) · a predicted model of the same protein · chain E against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P01579
- Every structure of UniProt P15260
- Every structure of UniProt P38484
- Elsewhere: RCSB PDB 6E3K · PDBe 6E3K · UniProt P01579 · UniProt P15260 · UniProt P38484
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