Research workbench

Staphylococcus aureus ftsz-GDP R29A mutant in R state

Analyse Staphylococcus aureus ftsz-GDP R29A mutant in R state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5H5I
Type: protein
Length: 305 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsz
UniProt: Q6GHP9
Ligands: GDP
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsz	protein	305	45% helix, 26% strand	Q6GHP9

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

2 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	391	0.65	0.79	55	empty
2	194	0.52	0.78	35	GDP

Compared structures

5H5I · Staphylococcus aureus FtsZ-GDP R29A mutant in R state · the same entry in another collection · chain A against A, TM-score 1.00
Q6GHP9 · AlphaFold monomer V2.0 prediction for cell division protein ftsz (Q6GHP9) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q6GHP9
Elsewhere: RCSB PDB 5H5I · PDBe 5H5I · UniProt Q6GHP9

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