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Ssx structure of metallo beta-lactamase L1 with one zinc in the active site

Analyse Ssx structure of metallo beta-lactamase L1 with one zinc in the active site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7UHT
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 0.38

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative metallo-beta-lactamase L1 (beta-lactamase type II) (ec 3.5.2.6) (penicillinase) (EC 3.5.2.6)protein26431% helix, 23% strandB2FTM1

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11080.380.7524ZN

Compared structures

  • 7UHT · SSX Structure of Metallo Beta-Lactamase L1 with One Zinc in the Active Site · the same entry in another collection · chain A against A, TM-score 1.00

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