6XS5
Crystal structure of human Vps29 complexed with RaPID-derived cyclic peptide RT-D1
Summary for 6XS5
Entry DOI | 10.2210/pdb6xs5/pdb |
Descriptor | Vacuolar protein sorting-associated protein 29, 48V-DTY-ILE-ILE-ASP-THR-PRO-LEU-GLY-VAL-PHE-LEU-SER-SER-LEU-LYS-ARG, GLYCEROL, ... (5 entities in total) |
Functional Keywords | vps29, retromer, endosome, protein transport, cyclic peptide, inhibitor, protein transport-inhibitor complex, protein transport/inhibitor |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 2 |
Total formula weight | 23851.45 |
Authors | Chen, K.-E.,Guo, Q.,Collins, B.M. (deposition date: 2020-07-15, release date: 2021-07-14, Last modification date: 2023-10-18) |
Primary citation | Chen, K.E.,Guo, Q.,Hill, T.A.,Cui, Y.,Kendall, A.K.,Yang, Z.,Hall, R.J.,Healy, M.D.,Sacharz, J.,Norwood, S.J.,Fonseka, S.,Xie, B.,Reid, R.C.,Leneva, N.,Parton, R.G.,Ghai, R.,Stroud, D.A.,Fairlie, D.P.,Suga, H.,Jackson, L.P.,Teasdale, R.D.,Passioura, T.,Collins, B.M. De novo macrocyclic peptides for inhibiting, stabilizing, and probing the function of the retromer endosomal trafficking complex. Sci Adv, 7:eabg4007-eabg4007, 2021 Cited by PubMed: 34851660DOI: 10.1126/sciadv.abg4007 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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