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The crystal structure of VREH2 mutant M263N

Analyse The crystal structure of VREH2 mutant M263N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5Y6Y
Type: protein
Length: 318 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epoxide hydrolase
UniProt: A0A0R5NGA4
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Epoxide hydrolase	protein	318	43% helix, 16% strand	A0A0R5NGA4

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	395	0.79	0.88	45	empty

Compared structures

5Y6Y · The crystal structure of VrEH2 mutant M263N · the same entry in another collection · chain B against B, TM-score 1.00

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 A0A0R5NGA4
Elsewhere: RCSB PDB 5Y6Y · PDBe 5Y6Y · UniProt A0A0R5NGA4

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