GL1X · GenesisL1 explorer

Research workbench

Crystal structure of a papain-fold protein without the catalytic cysteine from seeds of pachyrhizus erosus

Analyse Crystal structure of a papain-fold protein without the catalytic cysteine from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2B1N
Type
protein
Length
232 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SPE31; Peptide (LYS)(ALA)(SER)(VAL)(GLY)
Ligands
NAG, FUC

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASPE31protein22726% helix, 23% strand—
BPeptide (LYS)(ALA)(SER)(VAL)(GLY)protein50% helix, 0% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • FUC · alpha-L-fucopyranose · sugar · chains A

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

Interfaces

1 interface between chains.

  • A–B · 434 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 2B1N · Crystal structure of a papain-fold protein without the catalytic cysteine from seeds of… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.