7FJD: Membrane protein(WT)
Cryo-EM structure of a membrane protein(WT). Determined by electron microscopy at 3.2 Å resolution. Released 27 Jul 2022.
- Method
- Electron microscopy
- Resolution
- 3.2 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 8,352
- Mol. weight
- 189.56 kDa
- Ligands
- CLR
- Released
- 27 Jul 2022
Explore 7FJD in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7FJD contains 19 α-helices and 77 β-strands across 8 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.
Chains a and b: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 30-53 | 24 | |
Chain d: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-27 | 2 | 1 |
| β-strand | 32-36 | 5 | 1 |
| β-strand | 42-46 | 5 | 2 |
| β-strand | 51 | 1 | 1 |
| β-strand | 57-62 | 6 | 1 |
| α-helix | 63-65 | 3 | |
| β-strand | 68-72 | 5 | 2 |
| α-helix | 77-79 | 3 | |
| β-strand | 85-91 | 7 | 2 |
| β-strand | 97-98 | 2 | 3 |
| α-helix | 103-125 | 23 | |
Chain e: 2 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 37-40 | 4 | 4 |
| β-strand | 44-48 | 5 | 4 |
| β-strand | 57-61 | 5 | 2 |
| β-strand | 65-66 | 2 | 2 |
| β-strand | 75-77 | 3 | 4 |
| β-strand | 81-85 | 5 | 4 |
| β-strand | 95-100 | 6 | 2 |
| α-helix | 105-107 | 3 | |
| β-strand | 111-116 | 6 | 2 |
| β-strand | 122-123 | 2 | 3 |
| α-helix | 127-153 | 27 | |
Chain f: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 37-41 | 5 | 5 |
| β-strand | 44-48 | 5 | 5 |
| β-strand | 57-61 | 5 | 6 |
| β-strand | 75-76 | 2 | 5 |
| β-strand | 81-85 | 5 | 5 |
| β-strand | 94-100 | 7 | 6 |
| α-helix | 105-107 | 3 | |
| β-strand | 111-117 | 7 | 6 |
| β-strand | 122-124 | 3 | 7 |
| α-helix | 129-141 | 13 | |
| α-helix | 144-153 | 10 | |
Chain g: 2 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 31-34 | 4 | 8 |
| β-strand | 41-46 | 6 | 8 |
| β-strand | 53-57 | 5 | 6 |
| β-strand | 60-65 | 6 | 6 |
| β-strand | 71-76 | 6 | 8 |
| α-helix | 77-79 | 3 | |
| β-strand | 82-88 | 7 | 6 |
| β-strand | 93 | 1 | 6 |
| β-strand | 97-103 | 7 | 6 |
| β-strand | 107-109 | 3 | 7 |
| α-helix | 112-137 | 26 | |
Chain m: 2 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 33-36 | 4 | 9 |
| β-strand | 41-46 | 6 | 10 |
| β-strand | 54-60 | 7 | 11 |
| β-strand | 67-72 | 6 | 11 |
| β-strand | 83-88 | 6 | 10 |
| β-strand | 93-98 | 6 | 10 |
| β-strand | 108-114 | 7 | 11 |
| β-strand | 121-122 | 2 | 11 |
| β-strand | 126-127 | 2 | 11 |
| β-strand | 128-131 | 4 | 9 |
| β-strand | 140-143 | 4 | 12 |
| β-strand | 153-158 | 6 | 12 |
| β-strand | 174-176 | 3 | 12 |
| β-strand | 180-184 | 5 | 13 |
| β-strand | 189-193 | 5 | 13 |
| β-strand | 195-198 | 4 | 12 |
| β-strand | 219 | 1 | 12 |
| α-helix | 232-234 | 3 | |
| α-helix | 241-272 | 32 | |
Chain n: 5 helices, 26 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 24-26 | 3 | 14 |
| β-strand | 29-33 | 5 | 15 |
| β-strand | 38-40 | 3 | 16 |
| β-strand | 41-43 | 3 | 14 |
| β-strand | 51-56 | 6 | 15 |
| β-strand | 63-70 | 8 | 15 |
| β-strand | 73-76 | 4 | 15 |
| β-strand | 83-85 | 3 | 16 |
| β-strand | 92 | 1 | 14 |
| β-strand | 95-97 | 3 | 16 |
| α-helix | 102-104 | 3 | |
| β-strand | 106-109 | 4 | 15 |
| β-strand | 112 | 1 | 15 |
| β-strand | 129-133 | 5 | 15 |
| β-strand | 140 | 1 | 17 |
| β-strand | 143-147 | 5 | 18 |
| α-helix | 148-150 | 3 | |
| α-helix | 151-156 | 6 | |
| β-strand | 159-169 | 11 | 18 |
| β-strand | 170 | 1 | 17 |
| β-strand | 174-180 | 7 | 19 |
| β-strand | 183-184 | 2 | 19 |
| β-strand | 189-191 | 3 | 18 |
| β-strand | 196-197 | 2 | 18 |
| β-strand | 207-216 | 10 | 18 |
| α-helix | 217-220 | 4 | |
| β-strand | 226-233 | 8 | 19 |
| β-strand | 236 | 1 | 20 |
| β-strand | 250 | 1 | 20 |
| β-strand | 252-259 | 8 | 19 |
| α-helix | 270-307 | 38 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| T-cell surface glycoprotein CD3 zeta chain | a, b | protein | 165 | Homo sapiens | P20963 (AlphaFold model) |
| T-cell surface glycoprotein CD3 delta chain | d | protein | 171 | Homo sapiens | P04234 (AlphaFold model) |
| T-cell surface glycoprotein CD3 epsilon chain | e, f | protein | 207 | Homo sapiens | P07766 (AlphaFold model) |
| T-cell surface glycoprotein CD3 gamma chain | g | protein | 182 | Homo sapiens | P09693 (AlphaFold model) |
| T cell receptor alpha variable 12-3,Possible J 11 gene segment,T cell receptor alpha chain constant | m | protein | 272 | Homo sapiens | A0A0B4J271, A0N4Z6, P01848 |
| T cell receptor beta variable 6-5,M1-specific T cell receptor beta chain,T cell receptor beta… | n | protein | 312 | Homo sapiens | A0A0K0K1A5, P0DSE2 |
Sequence of entity 1 (a, b), FASTA
>7FJD_1 T-cell surface glycoprotein CD3 zeta chain (chains a, b)
MKWKALFTAAILQAQLPITEAQSFGLLDPKLCYLLDGILFIYGVILTALFLRVKFSRSAD
APAYQQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPQRRKNPQEGLYNELQKDKMA
EAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPRS
Sequence of entity 2 (d), FASTA
>7FJD_2 T-cell surface glycoprotein CD3 delta chain (chains d)
MEHSTFLSGLVLATLLSQVSPFKIPIEELEDRVFVNCNTSITWVEGTVGTLLSDITRLDL
GKRILDPRGIYRCNGTDIYKDKESTVQVHYRMCQSCVELDPATVAGIIVTDVIATLLLAL
GVFCFAGHETGRLSGAADTQALLRNDQVYQPLRDRDDAQYSHLGGNWARNK
Sequence of entity 3 (e, f), FASTA
>7FJD_3 T-cell surface glycoprotein CD3 epsilon chain (chains e, f)
MQSGTHWRVLGLCLLSVGVWGQDGNEEMGGITQTPYKVSISGTTVILTCPQYPGSEILWQ
HNDKNIGGDEDDKNIGSDEDHLSLKEFSELEQSGYYVCYPRGSKPEDANFYLYLRARVCE
NCMEMDVMSVATIVIVDICITGGLLLLVYYWSKNRKAKAKPVTRGAGAGGRQRGQNKERP
PPVPNPDYEPIRKGQRDLYSGLNQRRI
Sequence of entity 4 (g), FASTA
>7FJD_4 T-cell surface glycoprotein CD3 gamma chain (chains g)
MEQGKGLAVLILAIILLQGTLAQSIKGNHLVKVYDYQEDGSVLLTCDAEAKNITWFKDGK
MIGFLTEDKKKWNLGSNAKDPRGMYQCKGSQNKSKPLQVYYRMCQNCIELNAATISGFLF
AEIVSIFVLAVGVYFIAGQDGVRQSRASDKQTLLPNDQLYQPLKDREDDQYSHLQGNQLR
RN
Sequence of entity 5 (m), FASTA
>7FJD_5 T cell receptor alpha variable 12-3,Possible J 11 gene segment,T cell receptor alpha chain constant (chains m)
MKSLRVLLVILWLQLSWVWSQQKEVEQDPGPLSVPEGAIVSLNCTYSNSAFQYFMWYRQY
SRKGPELLMYTYSSGNKEDGRFTAQVDKSSKYISLFIRDSQPSDSATYLCAMSKGYSTLT
FGKGTMLLVSPDIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTV
LDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESSCDVKLVEKSFETDTN
LNFQNLSVIGFRILLLKVAGFNLLMTLRLWSS
Sequence of entity 6 (n), FASTA
>7FJD_6 T cell receptor beta variable 6-5,M1-specific T cell receptor beta chain,T cell receptor beta constant 2 (chains n)
MSISLLCCAALSLLWAGPVNAGVTQTPKFQVLKTGQSMTLQCAQDMNHEYMSWYRQDPGM
GLRLIHYSVGAGITDQGEVPNGYNVSRSTTEDFPLRLLSAAPSQTSVYFCASRRRQGASG
EQYFGPGTRLTVTEDLKNVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWV
NGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSEND
EWTQDRAKPVTQIVSAEAWGRADCGFTSESYQQGVLSATILYEILLGKATLYAVLVSALV
LMAMVKRKDSRG
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CLR | Cholesterol | C27 H46 O | 2 |
Primary citation
Cholesterol inhibits TCR signaling by directly restricting TCR-CD3 core tunnel motility. Chen, Y., Zhu, Y., Li, X. et al. Mol Cell (2022) 82:1278-1287.e5. DOI 10.1016/j.molcel.2022.02.017 · PubMed
Other PDB entries of the same protein (UniProt P20963 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2OQ1 1.9 Å, Tandem SH2 domains of ZAP-70 with 19-mer zeta1 peptide
- 3IK5 2.05 Å, SIVmac239 Nef in complex with TCR zeta ITAM 1 polypeptide (A63-R80)
- 8ES8 2.65 Å, CryoEM structure of PN45545 TCR-CD3 in complex with HLA-A2 MAGEA4 (230-239)
- 4XZ1 2.8 Å, ZAP-70-tSH2:Compound-B adduct
- 1YGR 2.9 Å, Crystal structure of the tandem phosphatase domain of RPTP CD45
- 7FJE 3.0 Å, Cryo-EM structure of a membrane protein(LL)
- 9CI8 3.01 Å, T cell receptor complex
- 8ES7 3.04 Å, CryoEM structure of PN45545 TCR-CD3 complex
- 7PHR 3.08 Å, Structure of a fully assembled T-cell receptor engaging a tumor-associated peptide-MHC I
- 9JY1 3.08 Å, delta epsilon/delta epsilon Fab-TCR tetramer
- 7FJF 3.1 Å, Cryo-EM structure of a membrane protein(CS)
- 8TW6 3.1 Å, TCR in nanodisc ND-II
Browse structure collections
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