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Fez-1 metallo-beta-lactamase from legionella gormanii modelled with unknown ligand

Analyse Fez-1 metallo-beta-lactamase from legionella gormanii modelled with unknown… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5W90
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fez-1 protein
EC: 3.5.2.6
UniProt: Q9K578
Ligands: UNL, ZN, SO4
Pockets: 1 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fez-1 protein (EC 3.5.2.6)	protein	263	34% helix, 25% strand	Q9K578

Ligands and binding sites

UNL · Unknown ligand · ligand · 2 copies · chains A
ZN · Zinc ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	95	0.41	0.78	23	ZN, UNL

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5W90 · FEZ-1 metallo-beta-lactamase from Legionella gormanii modelled with unknown ligand · the same entry in another collection · chain A against A, 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 Q9K578
Elsewhere: RCSB PDB 5W90 · PDBe 5W90 · UniProt Q9K578

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