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15K X-ray ligand free: exploring the mechanism of beta-lactam ring protonation in the class a beta-lactamase acylation mechanism using neutron and X-ray crystallography

Analyse 15K X-ray ligand free: exploring the mechanism of beta-lactam ring protonation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5A91
Type: protein
Length: 260 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
EC: 3.5.2.6
UniProt: E1ANH6
Ligands: SO4
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	(EC 3.5.2.6)	protein	260	42% helix, 18% strand	E1ANH6

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 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	67	0.30	0.75	17	SO4

Compared structures

5A91 · 15K X-ray ligand free: Exploring the Mechanism of beta-Lactam Ring Protonation in the… · the same entry in another collection · chain A against A, TM-score 1.00
E1ANH6 · AlphaFold monomer V2.0 prediction for beta-lactamase ctx-M-97 (E1ANH6) · a predicted model of the same protein · 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 E1ANH6
Elsewhere: RCSB PDB 5A91 · PDBe 5A91 · UniProt E1ANH6

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