Research workbench

aFtsz-GDP-Wat

Analyse aFtsz-GDP-Wat in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RVN
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.242
Source: Staphylococcus aureus
Molecule: Cell division protein FtsZ
UniProt: P0A031
Ligands: GDP, CA
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · resolution 1.242 · 1 distinct chain · 45% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein FtsZ	protein	308	45% helix, 24% strand	P0A031

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
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	255	0.60	0.80	41	GDP
2	110	0.49	0.81	16	empty
3	91	0.39	0.76	18	empty

Compared structures

6RVN · Aftsz-GDP-wat · the same entry in another collection · chain A against A, TM-score 1.00
P0A031 · AlphaFold monomer V2.0 prediction for cell division protein ftsz (P0A031) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 P0A031
Elsewhere: RCSB PDB 6RVN · PDBe 6RVN · UniProt P0A031

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