Research workbench

Cutr flat hexamer, form 1

Analyse Cutr flat hexamer, form 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XPI
Type: protein
Length: 649 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ethanolamine utilization protein euts
UniProt: A0A0E2IV13
Pockets: 1 · best druggability 0.71

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, F	Ethanolamine utilization protein euts	protein	108	35% helix, 36% strand	A0A0E2IV13
E	Ethanolamine utilization protein euts	protein	109	33% helix, 36% strand	A0A0E2IV13

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	886	0.71	0.77	90	empty

Interfaces

15 interfaces between chains.

E–F · 1382 Å² buried · 20 hydrogen bonds · protein-protein
D–E · 1354 Å² buried · 19 hydrogen bonds · protein-protein
C–D · 1336 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1334 Å² buried · 20 hydrogen bonds · protein-protein
A–F · 1329 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

6XPI · CutR flat hexamer, form 1 · 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 6XPI · PDBe 6XPI · UniProt A0A0E2IV13

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