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Crystal structure of the metallo beta lactamase L1 from stenotrophomonas maltophilia determined by serial crystallography

Analyse Crystal structure of the metallo beta lactamase L1 from stenotrophomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7L52
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative metallo-beta-lactamase L1 (beta-lactamase type II) (ec 3.5.2.6) (penicillinase)
EC: 3.5.2.6
UniProt: B2FTM1
Ligands: ZN
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative metallo-beta-lactamase L1 (beta-lactamase type II) (ec 3.5.2.6) (penicillinase) (EC 3.5.2.6)	protein	264	31% helix, 23% strand	B2FTM1

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

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	155	0.45	0.75	23	ZN

Compared structures

7L52 · Crystal Structure of the Metallo Beta Lactamase L1 from Stenotrophomonas maltophilia… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt B2FTM1
Elsewhere: RCSB PDB 7L52 · PDBe 7L52 · UniProt B2FTM1

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