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Crystal structure of the ig-C2 type 1 domain from mouse fibroblast growth factor receptor 2 (FGFR2) [nysgrc-005912]
Analyse Crystal structure of the ig-C2 type 1 domain from mouse fibroblast growth… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HWU
- Type
- protein
- Length
- 154 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibroblast growth factor receptor 2
- EC
- 2.7.10.1
- UniProt
- P21803
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor receptor 2 (EC 2.7.10.1) | protein | 81 | 4% helix, 54% strand | P21803 |
| B | Fibroblast growth factor receptor 2 (EC 2.7.10.1) | protein | 73 | 4% helix, 53% strand | P21803 |
Interfaces
1 interface between chains.
- A–B · 542 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4HWU · Crystal structure of the Ig-C2 type 1 domain from mouse Fibroblast growth factor receptor… · the same entry in another collection · chain A against A, TM-score 1.00
- P21803 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 2 (P21803) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 P21803
- Elsewhere: RCSB PDB 4HWU · PDBe 4HWU · UniProt P21803
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