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Ftsz gmpcpp soak I213 (M. jannaschii)

Analyse Ftsz gmpcpp soak I213 (M. jannaschii) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W58
Type: protein
Length: 337 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein ftsz homolog 1
UniProt: Q57816
Ligands: G2P, MG
Pockets: 4 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
1	Cell division protein ftsz homolog 1	protein	337	44% helix, 23% strand	Q57816

Ligands and binding sites

G2P · Phosphomethylphosphonic acid guanylate ester · ligand · chains 1
MG · Magnesium ion · metal · chains 1

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

Pockets

4 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	186	0.49	0.77	33	G2P, MG
2	158	0.46	0.76	26	empty
3	80	0.44	0.80	19	empty
4	52	0.28	0.75	16	empty

Compared structures

1W58 · FtsZ GMPCPP soak I213 (M. jannaschii) · the same entry in another collection · chain 1 against 1, TM-score 1.00
Q57816 · AlphaFold monomer V2.0 prediction for cell division protein ftsz 1 (Q57816) · a predicted model of the same protein · chain 1 against A, TM-score 0.95

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 Q57816
Elsewhere: RCSB PDB 1W58 · PDBe 1W58 · UniProt Q57816

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