Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6TL0

Solution structure and 1H, 13C and 15N chemical shift assignments for the complex of VPS29 with VARP 687-747

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005829cellular_componentcytosol
A0006886biological_processintracellular protein transport
A0006896biological_processGolgi to vacuole transport
A0010008cellular_componentendosome membrane
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0030904cellular_componentretromer complex
A0030906cellular_componentretromer, cargo-selective complex
A0032456biological_processendocytic recycling
A0042147biological_processretrograde transport, endosome to Golgi
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN B 1000
ChainResidue
BCYS711
BCYS715
BCYS717
BCYS720

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9UBQ0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues54
DetailsRegion: {"description":"Sufficient for interaction with VPS29","evidences":[{"source":"PubMed","id":"24856514","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

PDB statisticsPDBj update infoContact PDBjnumon