Research workbench

Crystal Structure of hFGFR2 D2 Domain

Analyse Crystal Structure of hFGFR2 D2 Domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CAF
Type: protein
Length: 100 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.96
Source: Homo sapiens
Molecule: Fibroblast growth factor receptor 2
EC: 2.7.10.1
UniProt: P21802

Structure

x-ray diffraction · resolution 1.96 · 1 distinct chain · 9% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fibroblast growth factor receptor 2 (EC 2.7.10.1)	protein	100	9% helix, 52% strand	P21802

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3CAF · Crystal structure of HFGFR2 D2 domain · the same entry in another collection · chain A against A, TM-score 1.00
P21802 · AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 2 (P21802) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P21802
Elsewhere: RCSB PDB 3CAF · PDBe 3CAF · UniProt P21802

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.