MolNFT v1 · #120927 · protein

Crystal structure of oxa-232 beta-lactamase

5HFO: “Crystal structure of oxa-232 beta-lactamase”. X-ray diffraction, 2 ligands (SO4, CL), 1 pocket (best druggability 0.78). MolNFT v1 #120927 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5HFO
Type: protein
Length: 489 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: M4JTK1
Ligands: SO4, CL
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase (EC 3.5.2.6)	protein	243	41% helix, 20% strand	M4JTK1
B	Beta-lactamase (EC 3.5.2.6)	protein	246	40% helix, 20% strand	M4JTK1

Ligands and binding sites

SO4 · Sulfate ion · ion · 7 copies · chains A, B
CL · Chloride ion · ion · chains A, B
GOL · Glycerol · additive · 5 copies · chains A, B

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	880	0.78	0.81	113	SO4, CL

Interfaces

1 interface between chains.

A–B · 1028 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (carboxylation).

Compared structures

5HFO · Crystal structure of oxa-232 beta-lactamase · 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 M4JTK1
Elsewhere: RCSB PDB 5HFO · PDBe 5HFO · UniProt M4JTK1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.