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Crystal structure of canavalia virosa lectin in complex with alpha- methyl-mannoside

Analyse Crystal structure of canavalia virosa lectin in complex with alpha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5F5Q
Type: protein
Length: 473 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Concanavalin-a
UniProt: P81461
Ligands: MMA, CA, MN

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Concanavalin-a	protein	237	4% helix, 48% strand	P81461
B	Concanavalin-a	protein	236	3% helix, 47% strand	P81461

Ligands and binding sites

MMA · methyl alpha-D-mannopyranoside · sugar · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B
MN · Manganese (II) ion · metal · 2 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 1163 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

5F5Q · Crystal structure of Canavalia virosa lectin in complex with alpha-methyl-mannoside · the same entry in another collection · chain A against A, TM-score 1.00
P81461 · AlphaFold monomer V2.0 prediction for concanavalin-a (P81461) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P81461
Elsewhere: RCSB PDB 5F5Q · PDBe 5F5Q · UniProt P81461

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