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Cutr dimer with domain swap

Analyse Cutr dimer with domain swap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XPH
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ethanolamine utilization protein euts
UniProt: A0A0E2IV13
Ligands: K, NA, SCN
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ethanolamine utilization protein euts	protein	99	40% helix, 32% strand	A0A0E2IV13

Ligands and binding sites

K · Potassium ion · metal · 2 copies · chains A, B
NA · Sodium ion · metal · chains A
SCN · Thiocyanate ion · ion · 2 copies · chains B
GOL · Glycerol · additive · 2 copies · chains A, B

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	462	0.71	0.80	39	GOL, SCN
2	56	0.43	0.83	21	empty

Interfaces

1 interface between chains.

A–B · 2058 Å² buried · 46 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6XPH · CutR dimer with domain swap · the same entry in another collection · chain B against B, 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 6XPH · PDBe 6XPH · UniProt A0A0E2IV13

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