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Horcolin complex with methyl-alpha-mannose

Analyse Horcolin complex with methyl-alpha-mannose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7V4S
Type: protein
Length: 143 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Horcolin
UniProt: Q5U9T2
Ligands: MMA

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 64% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Horcolin	protein	143	0% helix, 64% strand	Q5U9T2

Ligands and binding sites

MMA · methyl alpha-D-mannopyranoside · sugar · 2 copies · chains A

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

Compared structures

7V4S · Horcolin complex with methyl-alpha-mannose · the same entry in another collection · chain A against A, TM-score 1.00
Q5U9T2 · AlphaFold monomer V2.0 prediction for horcolin (Q5U9T2) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q5U9T2
Elsewhere: RCSB PDB 7V4S · PDBe 7V4S · UniProt Q5U9T2

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