7VT0: Dimer structure of SORLA

Dimer structure of SORLA. Determined by electron microscopy at 3.4 Å resolution. Released 2 Nov 2022.

Method: Electron microscopy
Resolution: 3.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 10,536
Mol. weight: 149.67 kDa
Released: 2 Nov 2022

Explore 7VT0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7VT0 contains 21 α-helices and 118 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: 10 helices, 61 β-strands

Element	Residues	Length	Sheet
β-strand	91-97	7	1
β-strand	104	1	2
β-strand	107-110	4	3
β-strand	116-119	4	3
β-strand	122	1	2
β-strand	136-137	2	4
β-strand	138	1	3
β-strand	146-147	2	4
α-helix	149-151	3
α-helix	160-162	3
β-strand	167-169	3	5
β-strand	177-180	4	5
β-strand	187-190	4	5
β-strand	208-211	4	6
β-strand	219-222	4	6
β-strand	231-234	4	6
β-strand	245	1	6
β-strand	248-252	5	7
β-strand	265-268	4	7
β-strand	277-280	4	7
α-helix	287-289	3
β-strand	290-294	5	7
β-strand	299-303	5	8
β-strand	306-312	7	8
β-strand	324-330	7	8
α-helix	345-346	2
β-strand	360-362	3	9
β-strand	372-374	3	9
β-strand	383-386	4	9
β-strand	389	1	10
β-strand	391	1	11
β-strand	412	1	11
β-strand	415-416	2	12
β-strand	424-425	2	12
β-strand	427	1	13
β-strand	428	1	10
β-strand	440	1	13
β-strand	442	1	14
β-strand	443	1	12
β-strand	451	1	14
β-strand	477	1	15
α-helix	493-494	2
β-strand	495	1	16
β-strand	504-507	4	16
β-strand	508	1	15
β-strand	519-523	5	16
β-strand	530	1	16
β-strand	534-535	2	16
β-strand	538-543	6	17
β-strand	548-553	6	17
β-strand	558	1	18
β-strand	560-561	2	19
β-strand	564	1	17
β-strand	574-575	2	19
β-strand	581	1	18
β-strand	583-587	5	1
β-strand	597-601	5	1
β-strand	611-616	6	1
α-helix	618-621	4
β-strand	623-624	2	20
α-helix	627-629	3
β-strand	633	1	21
β-strand	651	1	21
β-strand	660-661	2	20
β-strand	688-689	2	22
β-strand	700-701	2	22
α-helix	702	1
α-helix	703-705	3
β-strand	722-724	3	23
α-helix	730-731	2
β-strand	748-750	3	23

Chain B: 11 helices, 57 β-strands

Element	Residues	Length	Sheet
β-strand	91-97	7	24
β-strand	106-110	5	25
β-strand	116-121	6	25
β-strand	134-138	5	25
β-strand	146-147	2	25
α-helix	160-162	3
β-strand	167-169	3	26
β-strand	177-179	3	26
β-strand	186	1	27
β-strand	188-190	3	26
β-strand	197-198	2	26
β-strand	201	1	27
β-strand	208	1	28
β-strand	219-222	4	28
β-strand	230-234	5	28
β-strand	245-246	2	28
β-strand	248-252	5	29
α-helix	256-258	3
β-strand	264-268	5	29
β-strand	276-280	5	29
α-helix	287-289	3
β-strand	290-295	6	29
β-strand	297-303	7	30
β-strand	306-311	6	30
β-strand	325-330	6	30
α-helix	345-346	2
β-strand	350-353	4	31
β-strand	360-363	4	31
α-helix	366-368	3
β-strand	371-374	4	31
β-strand	383-386	4	31
β-strand	391	1	32
β-strand	412	1	32
β-strand	414-416	3	33
β-strand	424-426	3	33
β-strand	427	1	34
β-strand	440	1	34
β-strand	442	1	35
β-strand	443	1	33
β-strand	451	1	35
β-strand	475-477	3	36
α-helix	492-494	3
β-strand	495	1	37
β-strand	505	1	37
β-strand	506-510	5	36
β-strand	519-521	3	36
β-strand	534-535	2	36
β-strand	538-543	6	38
β-strand	548-553	6	38
β-strand	560-561	2	39
β-strand	564	1	38
β-strand	574-575	2	39
β-strand	583-587	5	24
β-strand	597-601	5	24
β-strand	611-616	6	24
α-helix	618-620	3
β-strand	623-624	2	40
β-strand	633	1	41
β-strand	651	1	41
β-strand	660-661	2	40
α-helix	679-681	3
α-helix	689	1
β-strand	690	1	42
α-helix	691	1
β-strand	699	1	42
α-helix	703-705	3
β-strand	722-724	3	43
β-strand	748-750	3	43

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Sortilin-related receptor	A, B	protein	664	Homo sapiens	Q92673 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7VT0_1 Sortilin-related receptor (chains A, B)
PIKVYGQVSLNDSHNQMVVHWAGEKSNVIVALARDSLALARPKSSDVYVSYDYGKSFKKI
SDKLNFGLGNRSEAVIAQFYHSPADNKRYIFADAYAQYLWITFDFCNTLQGFSIPFRAAD
LLLHSKASNLLLGFDRSHPNKQLWKSDDFGQTWIMIQEHVKSFSWGIDPYDKPNTIYIER
HEPSGYSTVFRSTDFFQSRENQEVILEEVRDFQLRDKYMFATKVVHLLGSEQQSSVQLWV
SFGRKPMRAAQFVTRHPINEYYIADASEDQVFVCVSHSNNRTNLYISEAEGLKFSLSLEN
VLYYSPGGAGSDTLVRYFANEPFADFHRVEGLQGVYIATLINGSMNEENMRSVITFDKGG
TWEFLQAPAFTGYGEKINCELSQGCSLHLAQRLSQLLNLQLRRMPILSKESAPGLIIATG
SVGKNLASKTNVYISSSAGARWREALPGPHYYTWGDHGGIITAIAQGMETNELKYSTNEG
ETWKTFIFSEKPVFVYGLLTEPGEKSTVFTIFGSNKENVHSWLILQVNATDALGVPCTEN
DYKLWSPSDERGNECLLGHKTVFKRRTPHATCFNGEDFDRPVVVSNCSCTREDYECDFGF
KMSEDLSLEVCVPDPEFSGKSYSPPVPCPVGSTYRRTRGYRKISGDTCSGGDVEARLEGE
LVPC

Primary citation

Cryo-EM structures reveal distinct apo conformations of sortilin-related receptor SORLA. Zhang, X., Wu, C., Song, Z. et al. Biochem Biophys Res Commun (2022) 600:75-79. DOI 10.1016/j.bbrc.2022.01.108 · PubMed

Other PDB entries of the same protein (UniProt Q92673 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3G2S 1.7 Å, VHS Domain of human GGA1 complexed with SorLA C-terminal Peptide
3G2T 2.0 Å, VHS Domain of human GGA1 complexed with SorLA C-terminal Phosphopeptide
3WSX 2.35 Å, SorLA Vps10p domain in ligand-free form
3WSY 3.11 Å, SorLA Vps10p domain in complex with its own propeptide fragment
3WSZ 3.2 Å, SorLA Vps10p domain in complex with Abeta-derived peptide
2DM4 Solution structure of the second fn3 domain of human sorLA/LR11

Browse structure collections

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