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Structure of remusatia vivipara lectin

Analyse Structure of remusatia vivipara lectin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3R0E
Type: protein
Length: 438 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lectin
UniProt: B5LYJ9
Pockets: 2 · best druggability 0.34

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Lectin	protein	109	0% helix, 43% strand	B5LYJ9
B, D	Lectin	protein	110	0% helix, 41% strand	B5LYJ9

Pockets

2 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	64	0.34	0.77	19	empty
2	72	0.34	0.76	18	empty

Interfaces

3 interfaces between chains.

A–B · 1746 Å² buried · 24 hydrogen bonds · protein-protein
C–D · 1727 Å² buried · 26 hydrogen bonds · protein-protein
B–D · 1109 Å² buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3R0E · Structure of Remusatia vivipara lectin · the same entry in another collection · chain A against A, TM-score 1.00
B5LYJ9 · AlphaFold monomer V2.0 prediction for mannose-specific lectin 1 (B5LYJ9) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 B5LYJ9
Elsewhere: RCSB PDB 3R0E · PDBe 3R0E · UniProt B5LYJ9

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