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Crystal structure of mgs-MCHE2, an ALPHA/BETA hydrolase enzyme from the metagenome of sediments from the lagoon of mar chica, morocco

Analyse Crystal structure of mgs-MCHE2, an ALPHA/BETA hydrolase enzyme from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JD6
Type: protein
Length: 219 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mgs-MCHE2
Pockets: 1 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mgs-MCHE2	protein	219	45% helix, 23% strand	—

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	127	0.41	0.75	21	empty

Compared structures

5JD6 · Crystal structure of MGS-MChE2, an alpha/beta hydrolase enzyme from the metagenome of… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 5JD6 · PDBe 5JD6

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