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Intriguing role of epoxide HYDROLASE/CYCLASE-like enzyme salbiii in pyran ring formation in polyether salinomycin

Analyse Intriguing role of epoxide HYDROLASE/CYCLASE-like enzyme salbiii in pyran ring… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CXO
Type: protein
Length: 263 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epoxide hydrolase
UniProt: H6D578
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epoxide hydrolase	protein	129	30% helix, 38% strand	H6D578
B	Epoxide hydrolase	protein	134	30% helix, 41% strand	H6D578

Ligands and binding sites

P6G · Hexaethylene glycol · additive · 5 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	170	0.62	0.84	24	P6G
2	155	0.60	0.83	24	P6G

Interfaces

1 interface between chains.

A–B · 1092 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

5CXO · Intriguing role of epoxide hydrolase/cyclase-like enzyme SalBIII in pyran ring formation… · the same entry in another collection · chain A against A, 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 H6D578
Elsewhere: RCSB PDB 5CXO · PDBe 5CXO · UniProt H6D578

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