MolNFT v1 · #164317 · protein

Copper oxidase from colletotrichum graminicola

6STX · Kelch domain-containing protein: “Copper oxidase from colletotrichum graminicola”. X-ray diffraction, 2 ligands (NAG, NA), 2 pockets (best druggability 0.66). MolNFT v1 #164317 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6STX
Type: protein
Length: 663 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kelch domain-containing protein
EC: 1.1.3.7
UniProt: E3Q9X3
Ligands: NAG, NA
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	Kelch domain-containing protein (EC 1.1.3.7)	protein	663	6% helix, 42% strand	E3Q9X3

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains C
NA · Sodium ion · metal · chains C
PG4 · Tetraethylene glycol · additive · chains C
ACT · Acetate ion · additive · chains C

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

Pockets

2 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	472	0.66	0.78	46	empty
2	93	0.38	0.76	17	empty

Modifications

Observed in the structure: 6 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

6STX · Copper oxidase from Colletotrichum graminicola · the same entry in another collection · chain C against C, 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 E3Q9X3
Elsewhere: RCSB PDB 6STX · PDBe 6STX · UniProt E3Q9X3

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