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Crystal structure of the family S1_7 ulvan-specific sulfatase FA22070 from formosa agariphila

Analyse Crystal structure of the family S1_7 ulvan-specific sulfatase FA22070 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HHM
Type: protein
Length: 459 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arylsulfatase
EC: 3.1.6.1
UniProt: T2KPK5
Ligands: CA
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Arylsulfatase (EC 3.1.6.1)	protein	459	33% helix, 19% strand	T2KPK5

Ligands and binding sites

CA · Calcium ion · metal · chains A

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

Pockets

3 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	283	0.54	0.75	32	empty
2	197	0.46	0.74	35	empty
3	88	0.37	0.76	16	empty

Compared structures

6HHM · Crystal structure of the family S1_7 ulvan-specific sulfatase FA22070 from Formosa… · the same entry in another collection · chain A against A, TM-score 1.00
T2KPK5 · AlphaFold monomer V2.0 prediction for ulvan-active sulfatase (T2KPK5) · a predicted model of the same protein · 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 T2KPK5
Elsewhere: RCSB PDB 6HHM · PDBe 6HHM · UniProt T2KPK5

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