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Ligand-free lectin from bauhinia forficata

Analyse Ligand-free lectin from bauhinia forficata in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T50
Type: protein
Length: 458 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lectin
UniProt: P86993
Ligands: CA
Pockets: 3 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lectin	protein	229	6% helix, 49% strand	P86993

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, B
EDO · 1,2-ethanediol · additive · 8 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	111	0.44	0.78	24	EDO
2	100	0.43	0.78	23	EDO
3	186	0.41	0.73	46	empty

Interfaces

1 interface between chains.

A–B · 863 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

5T50 · Ligand-free lectin from bauhinia forficata · the same entry in another collection · chain A against A, TM-score 1.00
P86993 · AlphaFold monomer V2.0 prediction for lectin (P86993) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P86993
Elsewhere: RCSB PDB 5T50 · PDBe 5T50 · UniProt P86993

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