Research workbench

Aquifex aeolicus ftsz with 8-morpholino-GTP

Analyse Aquifex aeolicus ftsz with 8-morpholino-GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2R75
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsz
UniProt: O66809
Ligands: 01G, MG
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
1	Cell division protein ftsz	protein	323	43% helix, 26% strand	O66809

Ligands and binding sites

01G · 8-morpholin-4-ylguanosine 5'-(tetrahydrogen triphosphate) · ligand · chains 1
MG · Magnesium ion · metal · chains 1

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

Pockets

3 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	208	0.51	0.77	37	MG, 01G
2	107	0.43	0.78	17	empty
3	67	0.32	0.75	17	empty

Compared structures

2R75 · Aquifex aeolicus FtsZ with 8-morpholino-GTP · the same entry in another collection · chain 1 against 1, TM-score 1.00
O66809 · AlphaFold monomer V2.0 prediction for cell division protein ftsz (O66809) · a predicted model of the same protein · chain 1 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 O66809
Elsewhere: RCSB PDB 2R75 · PDBe 2R75 · UniProt O66809

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