MolNFT v1 · #119085 · protein

Free state of ni-quercetinase

5FLH · Quercetinase qued: “Free state of ni-quercetinase”. X-ray diffraction, 2 ligands (NI, NO3), 5 pockets (best druggability 0.76). MolNFT v1 #119085 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5FLH
Type: protein
Length: 373 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Quercetinase qued
UniProt: A2VA43
Ligands: NI, NO3
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Quercetinase qued	protein	190	8% helix, 41% strand	A2VA43
B	Quercetinase qued	protein	183	10% helix, 42% strand	A2VA43

Ligands and binding sites

NI · Nickel (II) ion · metal · 2 copies · chains A, B
NO3 · Nitrate ion · ion · 3 copies · chains A, B
DMS · Dimethyl sulfoxide · additive · chains B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	154	0.76	0.93	33	NO3, DMS
2	107	0.73	0.93	28	empty
3	120	0.43	0.77	36	NO3
4	93	0.37	0.75	18	empty
5	92	0.37	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 1928 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

5FLH · Free state of Ni-quercetinase · 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 A2VA43
Elsewhere: RCSB PDB 5FLH · PDBe 5FLH · UniProt A2VA43

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