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Mycobacterium tuberculosis ftsz in complex with GTP-gamma-S

Analyse Mycobacterium tuberculosis ftsz in complex with GTP-gamma-S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RLU
Type: protein
Length: 598 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsz
UniProt: P64170
Ligands: GSP
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsz	protein	305	48% helix, 25% strand	P64170
B	Cell division protein ftsz	protein	293	44% helix, 25% strand	P64170

Ligands and binding sites

GSP · 5'-guanosine-diphosphate-monothiophosphate · ligand · chains A
GOL · Glycerol · additive · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	428	0.71	0.82	60	empty
2	441	0.64	0.78	57	GOL
3	201	0.51	0.77	34	GSP
4	112	0.40	0.76	25	empty

Interfaces

1 interface between chains.

A–B · 1113 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1RLU · Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S · the same entry in another collection · chain A against A, TM-score 1.00

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 P64170
Elsewhere: RCSB PDB 1RLU · PDBe 1RLU · UniProt P64170

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