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S. aureus FtsZ 12-316 F138A GDP Closed form (3FCm)

Analyse S. aureus FtsZ 12-316 F138A GDP Closed form (3FCm) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MN6
Type: protein
Length: 599 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.2
Source: Staphylococcus aureus
Molecule: Cell division protein FtsZ
UniProt: P0A031
Ligands: GDP
Pockets: 6 · best druggability 0.74

Structure

x-ray diffraction · resolution 3.2 · 2 distinct chains · 45% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein FtsZ	protein	296	45% helix, 24% strand	P0A031
B	Cell division protein FtsZ	protein	303	45% helix, 23% strand	P0A031

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1070	0.74	0.77	84	empty
2	250	0.54	0.77	38	GDP
3	203	0.53	0.78	38	GDP
4	138	0.53	0.81	28	empty
5	61	0.36	0.77	13	empty

Interfaces

1 interface between chains.

A–B · 254 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5MN6 · S. aureus ftsz 12-316 F138A GDP closed form (3FCM) · 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 B against A, TM-score 0.99

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 5MN6 · PDBe 5MN6 · UniProt P0A031

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