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Kinetic and structural characterization of the first B3 metallo-beta- lactamase with an active site glutamic acid

Analyse Kinetic and structural characterization of the first B3 metallo-beta- lactamase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LUU
Type: protein
Length: 266 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Subclass B3 metallo-beta-lactamase
UniProt: A0A1L5BQA7
Ligands: ZN, SO4
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Subclass B3 metallo-beta-lactamase	protein	266	33% helix, 24% strand	A0A1L5BQA7

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A
GOL · Glycerol · additive · 21 copies · 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	118	0.40	0.75	19	ZN, GOL

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7LUU · Kinetic and Structural Characterization of the First B3 Metallo-beta-Lactamase with an… · 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 A0A1L5BQA7
Elsewhere: RCSB PDB 7LUU · PDBe 7LUU · UniProt A0A1L5BQA7

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