Research workbench

Staphylococcus aureus ftsz apo-form (semet)

Analyse Staphylococcus aureus ftsz apo-form (semet) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VO9
Type: protein
Length: 1,175 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsz
UniProt: P0A029
Pockets: 13 · best druggability 0.83

Structure

x-ray diffraction · 4 distinct chains · 43% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsz	protein	295	44% helix, 24% strand	P0A029
B	Cell division protein ftsz	protein	292	43% helix, 24% strand	P0A029
C	Cell division protein ftsz	protein	301	44% helix, 23% strand	P0A029
D	Cell division protein ftsz	protein	287	43% helix, 24% strand	P0A029

Pockets

13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	449	0.83	0.90	42	empty
2	282	0.63	0.81	40	empty
3	56	0.62	0.93	25	empty
4	65	0.62	0.92	20	empty
5	406	0.59	0.76	39	empty

Interfaces

4 interfaces between chains.

B–D · 847 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 652 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 245 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 126 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 44 modified (engineered).

Compared structures

3VO9 · Staphylococcus aureus FtsZ apo-form (SeMet) · the same entry in another collection · chain D against D, TM-score 1.00
P0A029 · AlphaFold monomer V2.0 prediction for cell division protein ftsz (P0A029) · a predicted model of the same protein · chain B against A, TM-score 0.69

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 P0A029
Elsewhere: RCSB PDB 3VO9 · PDBe 3VO9 · UniProt P0A029

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