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Crystal structure of the cell-division protein ftsz at 2.8A resolution

Analyse Crystal structure of the cell-division protein ftsz at 2.8A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FSZ
Type: protein
Length: 334 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ftsz
UniProt: Q57816
Ligands: GDP
Pockets: 5 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ftsz	protein	334	43% helix, 23% strand	Q57816

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	177	0.49	0.77	34	GDP
2	71	0.40	0.79	17	empty
3	70	0.34	0.77	15	empty
4	68	0.31	0.74	15	empty
5	53	0.25	0.73	19	empty

Compared structures

1FSZ · Crystal structure of the cell-division protein ftsz at 2.8A resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q57816 · AlphaFold monomer V2.0 prediction for cell division protein ftsz 1 (Q57816) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q57816
Elsewhere: RCSB PDB 1FSZ · PDBe 1FSZ · UniProt Q57816

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