MolNFT v1 · #82472 · protein

Staphylococcus aureus ftsz 12-316 GDP-form

3VOA · Cell division protein ftsz: “Staphylococcus aureus ftsz 12-316 GDP-form”. X-ray diffraction, 2 ligands (GDP, CA), 3 pockets (best druggability 0.61). MolNFT v1 #82472 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3VOA
Type: protein
Length: 307 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsz
UniProt: P0A029
Ligands: GDP, CA
Pockets: 3 · best druggability 0.61

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsz	protein	307	45% helix, 24% strand	P0A029

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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	245	0.61	0.81	42	GDP
2	121	0.53	0.81	23	empty
3	101	0.41	0.77	23	empty

Compared structures

3VOA · Staphylococcus aureus FtsZ 12-316 GDP-form · the same entry in another collection · chain A against A, TM-score 1.00
P0A029 · AlphaFold monomer V2.0 prediction for cell division protein ftsz (P0A029) · 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 P0A029
Elsewhere: RCSB PDB 3VOA · PDBe 3VOA · UniProt P0A029

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