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MIM-2 Metallo-Beta-Lactamase

Analyse MIM-2 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: 6MFI
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.839
Source: Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1)
Molecule: Metallo-beta-lactamase
UniProt: K4KM71
Ligands: ZN
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · resolution 1.839 · 1 distinct chain · 34% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Metallo-beta-lactamase	protein	264	34% helix, 22% strand	K4KM71

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.41	0.77	32	ZN
2	60	0.34	0.77	17	empty
3	56	0.27	0.73	11	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6MFI · Mim-2 metallo-beta-lactamase · 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 K4KM71
Elsewhere: RCSB PDB 6MFI · PDBe 6MFI · UniProt K4KM71

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