GL1X · GenesisL1 explorer

Research workbench

Neuropilin-1 B1 domain in complex with EG01377; 2.8 ångström structure

Analyse Neuropilin-1 B1 domain in complex with EG01377; 2.8 ångström structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6FMF
Type
protein
Length
155 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Neuropilin-1
UniProt
O14786
Ligands
DUE

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANeuropilin-1protein1556% helix, 49% strandO14786

Ligands and binding sites

  • DUE · (2~{S})-2-[[3-[[5-[4-(aminomethyl)phenyl]-1-benzofuran-7-yl]sulfonylamino]thiophen-2-yl]carbonylamino]-5-carbamimidamido-pentanoic acid · ligand · chains A
  • TFA · trifluoroacetic acid · additive · chains A

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

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 6FMF · Neuropilin-1 b1 domain in complex with EG01377; 2.8 Angstrom structure · the same entry in another collection · chain A against A, TM-score 1.00
  • O14786 · AlphaFold monomer V2.0 prediction for neuropilin-1 (O14786) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

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