Research workbench

Oxa-48 carbapanemase, apo form

Analyse Oxa-48 carbapanemase, apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6P96
Type: protein
Length: 486 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
EC: 3.5.2.6
UniProt: Q6XEC0
Ligands: CA, CD, CL
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-lactamase (EC 3.5.2.6)	protein	243	41% helix, 21% strand	Q6XEC0

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A, B
CD · Cadmium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	918	0.78	0.81	122	CL
2	71	0.40	0.79	18	empty
3	62	0.37	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 1011 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

6P96 · OXA-48 carbapanemase, apo form · 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 Q6XEC0
Elsewhere: RCSB PDB 6P96 · PDBe 6P96 · UniProt Q6XEC0

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