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EGF

Analyse EGF in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2KV4
Type
protein
Length
53 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Epidermal growth factor
UniProt
Q6QBS2

Structure

solution nmr · 1 distinct chain · 17% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEpidermal growth factorprotein5317% helix, 8% strandQ6QBS2

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 2KV4 · EGF · the same entry in another collection · chain A against A, TM-score 1.00

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