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Crystal structure of ephrin A2 (EPHA2) receptor protein kinase with ags

Analyse Crystal structure of ephrin A2 (EPHA2) receptor protein kinase with ags in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5I9V
Type: protein
Length: 279 residues
Chains: 1
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
Ligands: AGS
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ephrin type-a receptor 2 (EC 2.7.10.1)	protein	279	41% helix, 19% strand	P29317

Ligands and binding sites

AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	314	0.66	0.81	35	AGS
2	71	0.32	0.75	20	empty

Compared structures

5I9V · Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with AGS · 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 A 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 5I9V · PDBe 5I9V · UniProt P29317

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