MolNFT v1 · #127118 · protein

S. aureus ftsz 12-316 F138A GDP open form (1FOF)

5MN4 · Cell division protein ftsz: “S. aureus ftsz 12-316 F138A GDP open form (1FOF)”. X-ray diffraction, 1 ligand (GDP), 3 pockets (best druggability 0.60). MolNFT v1 #127118 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5MN4
Type: protein
Length: 304 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsz
UniProt: P0A031
Ligands: GDP
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein ftsz	protein	304	47% helix, 24% strand	P0A031

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

3 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	226	0.60	0.81	41	GDP, MPD
2	70	0.37	0.78	16	empty
3	71	0.36	0.76	14	empty

Compared structures

5MN4 · S. aureus FtsZ 12-316 F138A GDP Open form (1FOf) · the same entry in another collection · chain A against A, TM-score 1.00
P0A031 · AlphaFold monomer V2.0 prediction for cell division protein ftsz (P0A031) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 P0A031
Elsewhere: RCSB PDB 5MN4 · PDBe 5MN4 · UniProt P0A031

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