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Mycobacterium tuberculosis ftsz in complex with GDP

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

PDB: 1RQ7
Type: protein
Length: 595 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsz
UniProt: P64170
Ligands: GDP
Pockets: 5 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsz	protein	300	46% helix, 25% strand	P64170
B	Cell division protein ftsz	protein	295	43% helix, 25% strand	P64170

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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	452	0.72	0.82	57	empty
2	203	0.52	0.78	31	empty
3	180	0.51	0.78	27	empty
4	177	0.50	0.77	37	empty
5	180	0.49	0.77	35	GDP

Interfaces

1 interface between chains.

A–B · 1112 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

1RQ7 · Mycobacterium tuberculosis ftsz in complex with GDP · 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 1RQ7 · PDBe 1RQ7 · UniProt P64170

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