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Crystal structure of the human EPHA4 ectodomain

Analyse Crystal structure of the human EPHA4 ectodomain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BK4
Type: protein
Length: 814 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ephrin type-a receptor 4
EC: 2.7.10.1
UniProt: P54764
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ephrin type-a receptor 4 (EC 2.7.10.1)	protein	514	0% helix, 36% strand	P54764
B	Ephrin type-a receptor 4 (EC 2.7.10.1)	protein	300	0% helix, 34% strand	P54764

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	709	0.65	0.74	52	empty
2	415	0.60	0.75	39	empty
3	231	0.59	0.80	31	empty
4	57	0.44	0.83	20	empty

Interfaces

1 interface between chains.

A–B · 501 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 disulfide (disulfide).

Compared structures

4BK4 · crystal structure of the human EphA4 ectodomain · the same entry in another collection · chain A against A, TM-score 1.00
P54764 · AlphaFold monomer V2.0 prediction for ephrin type-a receptor 4 (P54764) · a predicted model of the same protein · chain B against A, TM-score 0.94

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 P54764
Elsewhere: RCSB PDB 4BK4 · PDBe 4BK4 · UniProt P54764

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