Research workbench

Scoe with the caba substrate bound and HIS299 and ARG157 flipped out

Analyse Scoe with the caba substrate bound and HIS299 and ARG157 flipped out in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XN6
Type: protein
Length: 296 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Scoe protein
UniProt: A0A3B6UEU3
Ligands: 7UC, FE2, CL
Pockets: 2 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Scoe protein	protein	296	22% helix, 27% strand	A0A3B6UEU3

Ligands and binding sites

7UC · (3~{R})-3-(2-hydroxy-2-oxoethylamino)butanoic acid · ligand · chains A
FE2 · Fe (II) ion · metal · chains A
CL · Chloride ion · ion · chains A
ACT · Acetate ion · additive · 3 copies · chains A

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	286	0.84	0.95	50	7UC, ACT, FE2
2	55	0.27	0.74	19	empty

Compared structures

6XN6 · ScoE with the CABA substrate bound and His299 and Arg157 flipped out · 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 A0A3B6UEU3
Elsewhere: RCSB PDB 6XN6 · PDBe 6XN6 · UniProt A0A3B6UEU3

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