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Crystal structure of the class a beta-lactamase penl-TTR11 in complex with cba

Analyse Crystal structure of the class a beta-lactamase penl-TTR11 in complex with cba in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GLD
Type: protein
Length: 261 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: A0A2Z4SUB5
Ligands: CB4
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	261	44% helix, 21% strand	A0A2Z4SUB5

Ligands and binding sites

CB4 · Pinacol[[2-amino-alpha-(1-carboxy-1-methylethoxyimino)-4-thiazoleacetyl]amino]methaneboronate · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	286	0.54	0.76	44	CB4

Compared structures

5GLD · Crystal structure of the class A beta-lactamase PenL-tTR11 in complex with CBA · 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 A0A2Z4SUB5
Elsewhere: RCSB PDB 5GLD · PDBe 5GLD · UniProt A0A2Z4SUB5

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