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Dimeric sulfatase SPAS2 from silicibacter pomeroyi

Analyse Dimeric sulfatase SPAS2 from silicibacter pomeroyi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UPL
Type: protein
Length: 1,108 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sulfatase family protein
UniProt: Q5LMH0
Ligands: ZN
Pockets: 12 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sulfatase family protein	protein	555	39% helix, 17% strand	Q5LMH0
C	Sulfatase family protein	protein	553	39% helix, 17% strand	Q5LMH0

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, C

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

Pockets

12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	576	0.78	0.84	48	empty
2	515	0.78	0.85	49	empty
3	418	0.67	0.80	32	empty
4	238	0.66	0.83	47	empty
5	495	0.65	0.77	33	empty

Interfaces

1 interface between chains.

A–C · 5693 Å² buried · 83 hydrogen bonds · protein-protein

Compared structures

4UPL · Dimeric sulfatase SpAS2 from Silicibacter pomeroyi · 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 Q5LMH0
Elsewhere: RCSB PDB 4UPL · PDBe 4UPL · UniProt Q5LMH0

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