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Novel fungal alcohol oxidase with catalytic diversity among the AA5 family, in complex with copper

Analyse Novel fungal alcohol oxidase with catalytic diversity among the AA5 family, in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C92
Type: protein
Length: 481 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kelch domain-containing protein
UniProt: E3QHV8
Ligands: NAG, CU1
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kelch domain-containing protein	protein	481	2% helix, 40% strand	E3QHV8

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
CU1 · Copper (I) ion · metal · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.31	0.74	19	ACT

Modifications

Observed in the structure: 2 glycan, 1 disulfide (N-glycosylation, disulfide).

Compared structures

5C92 · Novel fungal alcohol oxidase with catalytic diversity among the AA5 family, in complex… · 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 E3QHV8
Elsewhere: RCSB PDB 5C92 · PDBe 5C92 · UniProt E3QHV8

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