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The crystal structure of canavalia maritima lectin (conm) in complex with trehalose and maltose

Analyse The crystal structure of canavalia maritima lectin (conm) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CYF
Type: protein
Length: 461 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lectin
Ligands: GLC, CA, MN
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lectin	protein	230	4% helix, 43% strand	—
C	Lectin	protein	231	4% helix, 45% strand	—

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, C
CA · Calcium ion · metal · 2 copies · chains A, C
MN · Manganese (II) ion · metal · 2 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	58	0.30	0.76	13	empty

Interfaces

1 interface between chains.

A–C · 1007 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

2CYF · The Crystal Structure of Canavalia Maritima Lectin (ConM) in Complex with Trehalose and… · 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
Elsewhere: RCSB PDB 2CYF · PDBe 2CYF

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