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Structure of cell filamentation protein (fic) from helicobacter pylori

Analyse Structure of cell filamentation protein (fic) from helicobacter pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F6S
Type: protein
Length: 360 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell filamentation protein, putative
Ligands: ZN, PO4
Pockets: 4 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cell filamentation protein, putative	protein	180	59% helix, 5% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

4 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	427	0.77	0.86	61	PO4
2	79	0.61	0.89	21	empty
3	67	0.57	0.88	20	empty
4	50	0.27	0.75	12	empty

Interfaces

1 interface between chains.

A–B · 1003 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

2F6S · Structure of cell filamentation protein (fic) from Helicobacter pylori · 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
Elsewhere: RCSB PDB 2F6S · PDBe 2F6S

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