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C-terminal domain of BC2L-C lectin from burkholderia cenocepacia

Analyse C-terminal domain of BC2L-C lectin from burkholderia cenocepacia in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XR4
Type: protein
Length: 232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lectin
UniProt: B4EH86
Ligands: SO4
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lectin	protein	116	0% helix, 56% strand	B4EH86

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

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	59	0.48	0.85	17	empty

Interfaces

1 interface between chains.

A–B · 1472 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

2XR4 · C-terminal domain of BC2L-C Lectin from Burkholderia cenocepacia · 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 B4EH86
Elsewhere: RCSB PDB 2XR4 · PDBe 2XR4 · UniProt B4EH86

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