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Crystal structure of metallo-beta-lactamase MBLBt2

Analyse Crystal structure of metallo-beta-lactamase MBLBt2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7FCT
Type: protein
Length: 477 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.8
Source: Bacillus phage vB_BtM_BMBsp2
Molecule: Metal beta-lactamase
UniProt: A0A4Y1LJC5
Ligands: ZN
Pockets: 4 · best druggability 0.62

Structure

x-ray diffraction · resolution 1.8 · 2 distinct chains · 27% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Metal beta-lactamase	protein	238	27% helix, 30% strand	A0A4Y1LJC5
B	Metal beta-lactamase	protein	239	28% helix, 29% strand	A0A4Y1LJC5

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A, B
GOL · Glycerol · additive · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	315	0.62	0.79	31	MPD
2	290	0.61	0.79	32	MPD
3	103	0.37	0.75	14	empty
4	73	0.31	0.73	23	empty

Interfaces

1 interface between chains.

A–B · 1366 Å² buried · 8 hydrogen bonds · protein-protein

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 A0A4Y1LJC5
Elsewhere: RCSB PDB 7FCT · PDBe 7FCT · UniProt A0A4Y1LJC5

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