Research workbench

C500S (T1D) mutant of cueo soaked in and bound to CU(I)

Analyse C500S (T1D) mutant of cueo soaked in and bound to CU(I) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NT0
Type: protein
Length: 468 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Blue copper oxidase cueo
UniProt: P36649
Ligands: CU1
Pockets: 5 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Blue copper oxidase cueo	protein	468	11% helix, 42% strand	P36649

Ligands and binding sites

CU1 · Copper (I) ion · metal · 9 copies · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	141	0.49	0.78	30	empty
2	63	0.46	0.84	20	empty
3	118	0.41	0.76	20	empty
4	63	0.31	0.75	16	empty
5	50	0.27	0.74	13	empty

Compared structures

3NT0 · C500S (T1D) Mutant of CueO soaked in and bound to Cu(I) · the same entry in another collection · chain A against A, TM-score 1.00
P36649 · AlphaFold monomer V2.0 prediction for blue copper oxidase cueo (P36649) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P36649
Elsewhere: RCSB PDB 3NT0 · PDBe 3NT0 · UniProt P36649

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