MolNFT v1 · #180600 · protein

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

7L52 · Putative metallo-beta-lactamase L1 (beta-lactamase type II)…: “Crystal structure of the metallo beta lactamase L1 from stenotrophomonas maltophilia determined by serial…”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best…

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

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 B2FTM1
Elsewhere: RCSB PDB 7L52 · PDBe 7L52 · UniProt B2FTM1

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