MolNFT v1 · #152013 · protein
Crystal structure of SOCS2:ELONGIN C:ELONGIN B in complex with erythropoietin receptor peptide
6I4X: “Crystal structure of SOCS2:ELONGIN C:ELONGIN B in complex with erythropoietin receptor peptide”. X-ray diffraction. MolNFT v1 #152013 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6I4X
- Type
- protein
- Length
- 356 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q15370, Q15369, O14508
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 103 | — | Q15370 |
| C | — | protein | 86 | — | Q15369 |
| A | — | protein | 158 | — | O14508 |
| D | — | protein | 9 | — | — |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains C, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6I4X · Crystal structure of SOCS2:Elongin C:Elongin B in complex with erythropoietin receptor… · the same entry in another collection · chain B against B, TM-score 1.00
- Q15370 · AlphaFold monomer V2.0 prediction for elongin-B (Q15370) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q15369 · AlphaFold monomer V2.0 prediction for elongin-C (Q15369) · a predicted model of the same protein · chain C against A, TM-score 0.98
- O14508 · AlphaFold monomer V2.0 prediction for suppressor of cytokine signaling 2 (O14508) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q15370
- Every structure of UniProt Q15369
- Every structure of UniProt O14508
- Elsewhere: RCSB PDB 6I4X · PDBe 6I4X · UniProt Q15370 · UniProt Q15369 · UniProt O14508
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