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Crystal structure of human epidermal growth factor

Analyse Crystal structure of human epidermal growth factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JL9
Type: protein
Length: 87 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epidermal growth factor
UniProt: P01133

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epidermal growth factor	protein	42	7% helix, 33% strand	P01133
B	Epidermal growth factor	protein	45	7% helix, 31% strand	P01133

Interfaces

1 interface between chains.

A–B · 362 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1JL9 · Crystal Structure of Human Epidermal Growth Factor · the same entry in another collection · chain A against A, TM-score 1.00
P01133 · AlphaFold monomer V2.0 prediction for pro-epidermal growth factor (P01133) · a predicted model of the same protein · chain A against A, TM-score 0.77

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 P01133
Elsewhere: RCSB PDB 1JL9 · PDBe 1JL9 · UniProt P01133

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