Research workbench

Cutr flat hexamer, form 2

Analyse Cutr flat hexamer, form 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XPJ
Type: protein
Length: 335 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ethanolamine utilization protein euts
UniProt: A0A0E2IV13
Ligands: SO4
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ethanolamine utilization protein euts	protein	109	35% helix, 34% strand	A0A0E2IV13
C	Ethanolamine utilization protein euts	protein	117	38% helix, 33% strand	A0A0E2IV13

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B, C

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	177	0.45	0.75	30	empty

Interfaces

3 interfaces between chains.

B–C · 1392 Å² buried · 20 hydrogen bonds · protein-protein
A–B · 1374 Å² buried · 21 hydrogen bonds · protein-protein
A–C · 150 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6XPJ · CutR flat hexamer, form 2 · 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 A0A0E2IV13
Elsewhere: RCSB PDB 6XPJ · PDBe 6XPJ · UniProt A0A0E2IV13

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