Research workbench

Structural basis for substrate recognition by a novel legionella phosphoinositide phosphatase

Analyse Structural basis for substrate recognition by a novel legionella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FYF
Type: protein
Length: 739 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sidf, inhibitor of growth family, member 3
EC: 3.1.3.67
UniProt: Q5ZSD5
Ligands: HG, PO4
Pockets: 10 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sidf, inhibitor of growth family, member 3 (EC 3.1.3.67)	protein	739	55% helix, 11% strand	Q5ZSD5

Ligands and binding sites

HG · Mercury (II) ion · metal · 3 copies · chains A
PO4 · Phosphate ion · ion · chains A

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

Pockets

10 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	776	0.75	0.80	66	PO4
2	238	0.67	0.84	41	empty
3	82	0.64	0.91	20	empty
4	430	0.62	0.77	42	HG
5	147	0.56	0.82	26	empty

Compared structures

4FYF · Structural basis for substrate recognition by a novel Legionella phosphoinositide… · 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 Q5ZSD5
Elsewhere: RCSB PDB 4FYF · PDBe 4FYF · UniProt Q5ZSD5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.