Research workbench
1:1 complex between an interferon gamma single-chain variant and its receptor
Analyse 1:1 complex between an interferon gamma single-chain variant and its receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FYH
- Type
- protein
- Length
- 884 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon gamma; Interferon gamma receptor 1
- UniProt
- P01579, P15260
- Ligands
- CL
- Pockets
- 11 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon gamma | protein | 242 | 71% helix, 0% strand | P01579 |
| B | Interferon gamma receptor 1 | protein | 201 | 5% helix, 49% strand | P15260 |
| D | Interferon gamma | protein | 240 | 71% helix, 0% strand | P01579 |
| E | Interferon gamma receptor 1 | protein | 201 | 5% helix, 49% strand | P15260 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 377 | 0.72 | 0.84 | 53 | empty |
| 2 | 204 | 0.65 | 0.84 | 34 | empty |
| 3 | 261 | 0.60 | 0.79 | 36 | empty |
| 4 | 306 | 0.59 | 0.77 | 36 | empty |
| 5 | 65 | 0.49 | 0.85 | 16 | empty |
Interfaces
5 interfaces between chains.
- D–E · 1023 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1012 Ų buried · 17 hydrogen bonds · protein-protein
- A–D · 490 Ų buried · 6 hydrogen bonds · protein-protein
- A–E · 392 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 384 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1FYH · 1:1 complex between an interferon gamma single-chain variant and its receptor · the same entry in another collection · chain E against E, TM-score 1.00
- P15260 · AlphaFold monomer V2.0 prediction for interferon gamma receptor 1 (P15260) · a predicted model of the same protein · chain E against A, TM-score 0.97
- P01579 · AlphaFold monomer V2.0 prediction for interferon gamma (P01579) · a predicted model of the same protein · chain D against A, TM-score 0.51
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
- Elsewhere: RCSB PDB 1FYH · PDBe 1FYH · UniProt P01579 · UniProt P15260
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