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Crystal structure of arabidopsis IDN2 xs domain along with a small segment of adjacent coiled-coil region

Analyse Crystal structure of arabidopsis IDN2 xs domain along with a small segment of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4E8U
Type: protein
Length: 331 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein T8P19.180
UniProt: Q9SMN2
Ligands: SO4
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein T8P19.180	protein	166	46% helix, 22% strand	Q9SMN2
C	Putative uncharacterized protein T8P19.180	protein	165	47% helix, 23% strand	Q9SMN2

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, 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	61	0.29	0.74	14	SO4

Interfaces

1 interface between chains.

A–C · 1087 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4E8U · Crystal structure of Arabidopsis IDN2 XS domain along with a small segment of adjacent… · 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 Q9SMN2
Elsewhere: RCSB PDB 4E8U · PDBe 4E8U · UniProt Q9SMN2

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