MolNFT v1 · #161070 · protein
Cryo-EM structure of RET/GFRA2/NRTN extracellular complex in the tetrameric form
6Q2R: “Cryo-EM structure of RET/GFRA2/NRTN extracellular complex in the tetrameric form”. Electron microscopy, 2 ligands (NAG, CA). MolNFT v1 #161070 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6Q2R
- Type
- protein
- Length
- 3,800 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q99748, O00451, P07949
- Ligands
- NAG, CA
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, U, V | — | protein | 98 | — | Q99748 |
| C, D, W, X | — | protein | 280 | — | O00451 |
| E, F, Y, Z | — | protein | 572 | — | P07949 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 24 copies · chains E, C, F, D, Y, W, Z, X
- CA · Calcium ion · metal · 16 copies · chains E, F, Y, Z
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6Q2R · Cryo-EM structure of RET/GFRa2/NRTN extracellular complex in the tetrameric form · the same entry in another collection · chain W against W, TM-score 1.00
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 Q99748
- Every structure of UniProt O00451
- Every structure of UniProt P07949
- Elsewhere: RCSB PDB 6Q2R · PDBe 6Q2R · UniProt Q99748 · UniProt O00451 · UniProt P07949
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