MolNFT v1 · #115086 · protein

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

5C92 · Kelch domain-containing protein: “Novel fungal alcohol oxidase with catalytic diversity among the AA5 family, in complex with copper”. X-ray diffraction, 2 ligands (NAG, CU1), 1 pocket (best druggability 0.31). MolNFT v1 #115086 on…

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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