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Structure of a streptococcus mutans CE4 esterase

Analyse Structure of a streptococcus mutans CE4 esterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W3Z
Type: protein
Length: 238 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative deacetylase
EC: 3.5.1.41
UniProt: Q8DV82
Ligands: ZN, PO4
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative deacetylase (EC 3.5.1.41)	protein	238	45% helix, 18% strand	Q8DV82

Ligands and binding sites

ZN · Zinc ion · metal · chains A
PO4 · Phosphate ion · ion · 2 copies · chains A

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

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	74	0.34	0.76	19	ZN, PO4

Compared structures

2W3Z · Structure of a Streptococcus mutans CE4 esterase · 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 Q8DV82
Elsewhere: RCSB PDB 2W3Z · PDBe 2W3Z · UniProt Q8DV82

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