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Crystal structure of cell division protein ftsy (TM0570) from thermotoga maritima at 1.60 a resolution

Analyse Crystal structure of cell division protein ftsy (TM0570) from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VMA
Type: protein
Length: 588 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsy
UniProt: Q9WZ40
Ligands: MG
Pockets: 6 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cell division protein ftsy	protein	294	54% helix, 14% strand	Q9WZ40

Ligands and binding sites

MG · Magnesium ion · metal · chains A
CIT · Citric acid · additive · chains B

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

Pockets

6 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	613	0.66	0.76	71	empty
2	65	0.43	0.81	14	empty
3	55	0.36	0.80	14	empty
4	59	0.36	0.78	15	empty
5	62	0.33	0.77	14	empty

Interfaces

1 interface between chains.

A–B · 1150 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1VMA · Crystal structure of Cell division protein ftsY (TM0570) from Thermotoga maritima at 1.60… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9WZ40
Elsewhere: RCSB PDB 1VMA · PDBe 1VMA · UniProt Q9WZ40

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