4PO7: Sortilin

Structure of the Sortilin:neurotensin complex at excess neurotensin concentration. Determined by X-ray diffraction at 2.66 Å resolution. Released 23 Jul 2014.

Method
X-ray diffraction
Resolution
2.66 Å
Organism
Homo sapiens
Chains
3
Atoms
5,518
Mol. weight
81.72 kDa
Ligands
NAG
Released
23 Jul 2014

Explore 4PO7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PO7 contains 19 α-helices and 67 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 19 helices, 65 β-strands

ElementResiduesLengthSheet
α-helix59-646
β-strand67-7261
β-strand78-8362
β-strand91-9662
β-strand9713
β-strand10813
β-strand111-11442
β-strand122-12322
α-helix125-1284
β-strand13314
β-strand139-14135
α-helix1421
β-strand149-15245
β-strand15314
α-helix1541
β-strand163-16755
β-strand175-17845
β-strand18316
β-strand188-19037
β-strand193-20087
β-strand20116
β-strand206-20947
β-strand217-22047
β-strand223-22868
α-helix230-2323
β-strand234-23858
β-strand25119
β-strand252-25658
β-strand264-26528
β-strand270-27679
β-strand279-28579
β-strand292-29769
β-strand305-30629
β-strand31219
β-strand318-323610
β-strand328-333610
α-helix3341
β-strand340-346710
β-strand353-361910
β-strand362111
β-strand369111
β-strand372-373210
β-strand381-386610
β-strand392-397610
β-strand404-406310
β-strand407112
α-helix408-4103
α-helix413-4153
β-strand426-429412
α-helix432-4365
β-strand446112
β-strand455-462812
α-helix469-4702
β-strand471-475512
β-strand483-486412
β-strand490-495613
α-helix496-4983
β-strand500-505613
β-strand51111
β-strand513-517513
β-strand525-528413
β-strand534-54071
β-strand549-55681
β-strand564-57071
α-helix571-5733
β-strand578114
α-helix581-5833
β-strand584-588515
β-strand602115
β-strand605-612815
α-helix6131
β-strand619114
β-strand628-632515
α-helix633-6342
β-strand635116
α-helix637-6393
β-strand640-642317
β-strand646-647218
β-strand656-657218
α-helix664-6718
α-helix674-6774
β-strand682-684317
β-strand693116
α-helix704-7085
Chain N: 0 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand2-432
β-strand11-12210

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
SortilinAprotein685Homo sapiensQ99523 (AlphaFold model)
Neurotensin/neuromedin NN, Pprotein13Homo sapiensP30990 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4PO7_1 Sortilin (chains A)
SAPGEDEECGRVRDFVAKLANNTHQHVFDDLRGSVSLSWVGDSTGVILVLTTFHVPLVIM
TFGQSKLYRSEDYGKNFKDITDLINNTFIRTEFGMAIGPENSGKVVLTAEVSGGSRGGRI
FRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLWVSKNFGGKWEEIHKAVC
LAKWGSDNTIFFTTYANGSCKADLGALELWRTSDLGKSFKTIGVKIYSFGLGGRFLFASV
MADKDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDMVFMHVDEPGDTGFGTIF
TSDDRGIVYSKSLDRHLYTTTGGETDFTNVTSLRGVYITSVLSEDNSIQTMITFDQGGRW
THLRKPENSECDATAKNKNECSLHIHASYSISQKLNVPMAPLSEPNAVGIVIAHGSVGDA
ISVMVPDVYISDDGGYSWTKMLEGPHYYTILDSGGIIVAIEHSSRPINVIKFSTDEGQCW
QTYTFTRDPIYFTGLASEPGARSMNISIWGFTESFLTSQWVSYTIDFKDILERNCEEKDY
TIWLAHSTDPEDYEDGCILGYKEQFLRLRKSSMCQNGRDYVVTKQPSICLCSLEDFLCDF
GYYRPENDSKCVEQPELKGHDLEFCLYGREEHLTTNGYRKIPGDKCQGGVNPVREVKDLK
KKCTSNFLSPEKQNSKSNSHHHHHH
Sequence of entity 2 (N, P), FASTA
>4PO7_2 Neurotensin/neuromedin N (chains N, P)
QLYENKPRRPYIL

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O61

Water and common crystallization additives (PG4) are not listed.

Primary citation

Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin. Quistgaard, E.M., Grftehauge, M.K., Madsen, P. et al. Protein Sci (2014) 23:1291-1300. DOI 10.1002/pro.2512 · PubMed

Other PDB entries of the same protein (UniProt Q99523 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 4PO7 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.