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Crystal structure of the M441L mutant of the multicopper oxidase cueo

Analyse Crystal structure of the M441L mutant of the multicopper oxidase cueo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PF3
Type: protein
Length: 463 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Blue copper oxidase cueo
UniProt: P36649
Ligands: C2C, CU
Pockets: 4 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Blue copper oxidase cueo	protein	463	12% helix, 42% strand	P36649

Ligands and binding sites

C2C · Cu-cl-Cu linkage · ligand · chains A
CU · Copper (II) ion · metal · 2 copies · chains A

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

Pockets

4 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	55	0.46	0.85	21	empty
2	123	0.43	0.76	22	empty
3	74	0.41	0.80	20	empty
4	76	0.34	0.75	19	empty

Compared structures

1PF3 · Crystal Structure of the M441L mutant of the multicopper oxidase CueO · 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 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 P36649
Elsewhere: RCSB PDB 1PF3 · PDBe 1PF3 · UniProt P36649

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