Research workbench

Thermotoga maritima FTSA:FTSZ(336-351)

Analyse Thermotoga maritima FTSA:FTSZ(336-351) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4A2A
Type: protein
Length: 778 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsa, putative; Cell division protein ftsz
UniProt: Q9WZU0, O08398
Ligands: ATP
Pockets: 8 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 38% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsa, putative	protein	372	37% helix, 33% strand	Q9WZU0
B	Cell division protein ftsa, putative	protein	377	37% helix, 33% strand	Q9WZU0
C	Cell division protein ftsz	protein	14	50% helix, 0% strand	O08398
D	Cell division protein ftsz	protein	15	47% helix, 0% strand	O08398

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B

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

Pockets

8 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	346	0.76	0.87	53	ATP
2	355	0.73	0.84	49	ATP
3	149	0.47	0.77	18	empty
4	230	0.46	0.73	33	empty
5	92	0.45	0.79	17	empty

Interfaces

3 interfaces between chains.

A–B · 702 Å² buried · 6 hydrogen bonds · protein-protein
B–D · 615 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 590 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4A2A · Thermotoga maritima FtsA:FtsZ(336-351) · the same entry in another collection · chain A against A, TM-score 1.00
O08398 · AlphaFold monomer V2.0 prediction for cell division protein ftsz (O08398) · a predicted model of the same protein · chain C against A, TM-score 0.48

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 Q9WZU0
Every structure of UniProt O08398
Elsewhere: RCSB PDB 4A2A · PDBe 4A2A · UniProt Q9WZU0 · UniProt O08398

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