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Structure of the autoinhibited EPHA2 jms-kd

Analyse Structure of the autoinhibited EPHA2 jms-kd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EK7
Type: protein
Length: 572 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ephrin type-a receptor 2
EC: 2.7.10.1
UniProt: P29317
Pockets: 4 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ephrin type-a receptor 2 (EC 2.7.10.1)	protein	286	40% helix, 16% strand	P29317

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	960	0.77	0.79	81	empty
2	451	0.65	0.78	52	empty
3	428	0.65	0.78	49	empty
4	63	0.28	0.73	10	empty

Interfaces

1 interface between chains.

A–B · 1088 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

5EK7 · Structure of the autoinhibited Epha2 JMS-KD · the same entry in another collection · chain A against A, TM-score 1.00
P29317 · AlphaFold monomer V2.0 prediction for ephrin type-a receptor 2 (P29317) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 P29317
Elsewhere: RCSB PDB 5EK7 · PDBe 5EK7 · UniProt P29317

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