MolNFT v1 · #141304 · protein

Crystal structure of the bacterial cell division protein ftsq and ftsb

5Z2W: “Crystal structure of the bacterial cell division protein ftsq and ftsb”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.42). MolNFT v1 #141304 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5Z2W
Type: protein
Length: 244 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsq; Cell division protein ftsb
UniProt: J7Q602, A0A1Q6B6Y5
Ligands: MG
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsq	protein	209	27% helix, 30% strand	J7Q602
B	Cell division protein ftsb	protein	35	37% helix, 14% strand	A0A1Q6B6Y5

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.42	0.82	17	empty
2	54	0.41	0.81	10	empty

Interfaces

1 interface between chains.

A–B · 964 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

5Z2W · Crystal structure of the bacterial cell division protein FtsQ and FtsB · the same entry in another collection · chain B against B, 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 J7Q602
Every structure of UniProt A0A1Q6B6Y5
Elsewhere: RCSB PDB 5Z2W · PDBe 5Z2W · UniProt J7Q602 · UniProt A0A1Q6B6Y5

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