Research workbench

Crystal structure of the ERBB4 kinase

Analyse Crystal structure of the ERBB4 kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BCE
Type: protein
Length: 857 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Receptor tyrosine-protein kinase erbb-4
EC: 2.7.10.1
UniProt: Q15303
Ligands: MN
Pockets: 8 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 38% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Receptor tyrosine-protein kinase erbb-4 (EC 2.7.10.1)	protein	285	38% helix, 19% strand	Q15303
B	Receptor tyrosine-protein kinase erbb-4 (EC 2.7.10.1)	protein	286	37% helix, 20% strand	Q15303
C	Receptor tyrosine-protein kinase erbb-4 (EC 2.7.10.1)	protein	286	38% helix, 20% strand	Q15303

Ligands and binding sites

MN · Manganese (II) ion · metal · chains A, C
PG4 · Tetraethylene glycol · additive · chains C
PEG · Di(hydroxyethyl)ether · additive · chains C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	450	0.67	0.79	46	empty
2	405	0.66	0.79	43	PEG
3	381	0.64	0.79	39	empty
4	369	0.62	0.78	47	empty
5	115	0.39	0.75	20	empty

Interfaces

2 interfaces between chains.

A–B · 439 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 341 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

3BCE · Crystal structure of the ErbB4 kinase · the same entry in another collection · chain A against A, TM-score 1.00
Q15303 · AlphaFold monomer V2.0 prediction for receptor tyrosine-protein kinase erbb-4 (Q15303) · a predicted model of the same protein · chain C 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 Q15303
Elsewhere: RCSB PDB 3BCE · PDBe 3BCE · UniProt Q15303

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