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Time-Resolved Structure of Metallo Beta-Lactamase L1 Before Reaction (Dark-Set)

Analyse Time-Resolved Structure of Metallo Beta-Lactamase L1 Before Reaction (Dark-Set) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7UHR
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.2
Source: Stenotrophomonas maltophilia K279a
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 0.41

Structure

x-ray diffraction · resolution 2.2 · 1 distinct chain · 28% 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	28% helix, 23% strand	B2FTM1

Ligands and binding sites

ZN · Zinc ion · metal · 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	127	0.41	0.75	28	ZN

Compared structures

7UHR · Time-resolved structure of metallo beta-lactamase L1 before reaction (dark-set) · 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 7UHR · PDBe 7UHR · UniProt B2FTM1

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