MolNFT v1 · #52346 · protein

The structure of ftsz from bacillus subtilis at 1.7A resolution

2VXY · Cell division protein ftsz: “The structure of ftsz from bacillus subtilis at 1.7A resolution”. X-ray diffraction, 1 ligand (K), 4 pockets (best druggability 0.54). MolNFT v1 #52346 on GenesisL1: 3D structure, binding sites and…

PDB: 2VXY
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsz
UniProt: P17865
Ligands: K
Pockets: 4 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsz	protein	306	44% helix, 25% strand	P17865

Ligands and binding sites

K · Potassium ion · metal · chains A
CIT · Citric acid · additive · chains A

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

Pockets

4 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	215	0.54	0.78	31	CIT
2	84	0.46	0.81	16	empty
3	77	0.34	0.75	22	K
4	64	0.34	0.76	15	empty

Compared structures

2VXY · The structure of FTsZ from Bacillus subtilis at 1.7A resolution · the same entry in another collection · chain A against A, TM-score 1.00
P17865 · AlphaFold monomer V2.0 prediction for cell division protein ftsz (P17865) · a predicted model of the same protein · chain A 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 P17865
Elsewhere: RCSB PDB 2VXY · PDBe 2VXY · UniProt P17865

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