Research workbench
Crystal structure of an asymmetric dimer of FGF receptor 3 kinases trapped in a-loop tyrosine transphosphorylation reaction
Analyse Crystal structure of an asymmetric dimer of FGF receptor 3 kinases trapped in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PNX
- Type
- protein
- Length
- 585 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22607
- Ligands
- ACP, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 291 | — | P22607 |
| B | — | protein | 294 | — | P22607 |
Ligands and binding sites
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PNX · Crystal Structure of an Asymmetric Dimer of FGF Receptor 3 Kinases Trapped in A-loop… · the same entry in another collection · chain A against A, TM-score 1.00
- P22607 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 3 (P22607) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P22607
- Elsewhere: RCSB PDB 6PNX · PDBe 6PNX · UniProt P22607
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