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The crystal structure of the zinc inhibited form of teicoplanin deacetylase Orf2

Analyse The crystal structure of the zinc inhibited form of teicoplanin deacetylase Orf2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DFM
Type: protein
Length: 266 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.01
Source: Actinoplanes teichomyceticus
Molecule: Teicoplanin pseudoaglycone deacetylase ORF2
UniProt: Q6ZZJ1
Ligands: ZN, SO4
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · resolution 2.01 · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Teicoplanin pseudoaglycone deacetylase ORF2	protein	266	44% helix, 16% strand	Q6ZZJ1

Ligands and binding sites

ZN · Zinc ion · metal · 5 copies · chains A
SO4 · Sulfate ion · ion · 2 copies · 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	521	0.69	0.79	59	SO4
2	78	0.32	0.74	19	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

3DFM · The crystal structure of the zinc inhibited form of teicoplanin deacetylase ORF2 · 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 Q6ZZJ1
Elsewhere: RCSB PDB 3DFM · PDBe 3DFM · UniProt Q6ZZJ1

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