MolNFT v1 · #177996 · protein

Structure of the G304E mutant of cueo

7F19 · Blue copper oxidase cueo: “Structure of the G304E mutant of cueo”. X-ray diffraction, 3 ligands (C2O, CU, NO3), 3 pockets (best druggability 0.50). MolNFT v1 #177996 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7F19
Type: protein
Length: 444 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Blue copper oxidase cueo
EC: 1.-.-.-
UniProt: W8T2X0
Ligands: C2O, CU, NO3
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Blue copper oxidase cueo (EC 1.-.-.-)	protein	444	7% helix, 44% strand	W8T2X0

Ligands and binding sites

C2O · Cu-O-Cu linkage · ligand · chains A
CU · Copper (II) ion · metal · 2 copies · chains A
NO3 · Nitrate ion · ion · 3 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A

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	128	0.50	0.80	29	empty
2	117	0.41	0.76	22	PEG
3	52	0.31	0.77	15	empty

Compared structures

7F19 · Structure of the G304E mutant of CueO · 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 W8T2X0
Elsewhere: RCSB PDB 7F19 · PDBe 7F19 · UniProt W8T2X0

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