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Structure of BT1596,A 2-O gag sulfatase

Analyse Structure of BT1596,A 2-O gag sulfatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5G2U
Type: protein
Length: 463 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2-O glycosaminoglycan sulfatase
EC: 3.1.6.18
UniProt: Q8A7C8
Ligands: ZN
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2-O glycosaminoglycan sulfatase (EC 3.1.6.18)	protein	463	36% helix, 15% strand	Q8A7C8

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CIT · Citric acid · additive · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	256	0.56	0.77	31	empty
2	136	0.52	0.81	29	CIT
3	115	0.50	0.80	20	empty

Compared structures

5G2U · Structure of BT1596,a 2-O GAG sulfatase · the same entry in another collection · chain A against A, TM-score 1.00
Q8A7C8 · AlphaFold monomer V2.0 prediction for delta 4,5-hexuronate-2-O-sulfatase (Q8A7C8) · 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 Q8A7C8
Elsewhere: RCSB PDB 5G2U · PDBe 5G2U · UniProt Q8A7C8

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