6MNO: 6235 TCR

6235 TCR bound to I-Ab Padi4. Determined by X-ray diffraction at 2.9 Å resolution. Released 3 Jul 2019.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Mus musculus
Chains
4
Atoms
6,133
Mol. weight
95.27 kDa
Released
3 Jul 2019

Explore 6MNO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6MNO contains 24 α-helices and 79 β-strands across 4 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: 4 helices, 22 β-strands

ElementResiduesLengthSheet
β-strand4-749
β-strand10-14510
α-helix181
β-strand19-2579
β-strand32-38710
β-strand45-51710
β-strand56-5949
β-strand62-6769
β-strand72-7769
α-helix82-843
β-strand86-90510
β-strand91-92211
β-strand93110
α-helix95-973
β-strand103-104211
β-strand108-113610
α-helix114-1152
β-strand122-125412
β-strand127113
β-strand135-140612
β-strand147114
β-strand156-159412
β-strand163-164215
β-strand176-180512
β-strand195114
β-strand201112
Chain B: 7 helices, 27 β-strands
ElementResiduesLengthSheet
β-strand2-5416
β-strand8-12517
β-strand17-18218
β-strand20-23416
β-strand29-36817
β-strand40-47817
β-strand54-55217
β-strand62-65418
β-strand71-72216
β-strand73-76418
α-helix81-833
β-strand85-92817
β-strand100-101217
β-strand105-110617
α-helix113-1153
β-strand117119
α-helix118-1192
β-strand120-124515
β-strand125113
α-helix126-1272
α-helix128-1347
β-strand136-1461115
β-strand147119
β-strand151-157720
β-strand160-162320
β-strand166-168315
β-strand173-174215
β-strand184-1931015
α-helix194-1974
β-strand203-210820
β-strand213121
α-helix224-2252
β-strand227121
β-strand229-236820
Chain C: 3 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand4-15121
β-strand19-2681
β-strand29-3571
β-strand40-4341
β-strand5312
α-helix56-7621
α-helix80-845
β-strand8813
β-strand91-9334
β-strand103-112104
β-strand118-12035
β-strand131-13444
α-helix136-1372
β-strand138-13924
β-strand145-15394
β-strand162-16655
β-strand174-17745
Chain D: 10 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand-2412
α-helix-18--163
β-strand7-18121
β-strand23-32101
β-strand35-4171
β-strand46-4941
α-helix52-543
α-helix55-639
α-helix65-7410
α-helix75-806
α-helix81-822
α-helix83-875
α-helix88-892
α-helix91-933
β-strand9616
α-helix97-982
β-strand99-10467
β-strand115-12397
β-strand12416
β-strand129-13468
β-strand13818
β-strand143-14537
β-strand149-15027
β-strand156-16387
β-strand171-17778
β-strand185-19068

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
H-2 class II histocompatibility antigen, A-B alpha chainCprotein179Mus musculusP14434 (AlphaFold model)
Padi4 (92-105) peptide and MHC Class II I-Ab beta chainDprotein217Mus musculusP14483 (AlphaFold model), Q9Z183 (AlphaFold model)
6235 TCR alpha chainAprotein208Mus musculus
6235 TCR beta chainBprotein239Mus musculus
Sequence of entity 1 (C), FASTA
>6MNO_1 H-2 class II histocompatibility antigen, A-B alpha chain (chains C)
IEADHVGTYGISVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFGQLASFDPQGG
LQNIAVVKHNLGVLTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINI
TWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHW
Sequence of entity 2 (D), FASTA
>6MNO_2 Padi4 (92-105) peptide and MHC Class II I-Ab beta chain (chains D)
RVSYYGPKTSPVQGGGGSLVPRGSGGGGSERHFVYQFMGECYFTNGTQRIRYVTRYIYNR
EEYVRYDSDVGEHRAVTELGRPDAEYWNSQPEILERTRAELDTVCRHNYEGPETHTSLRR
LEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDW
TFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWRA
Sequence of entity 3 (A), FASTA
>6MNO_3 6235 TCR alpha chain (chains A)
MQQVRQSPQSLTVWEGETAILNCSYENSAFDYFPWYQQFPGEGPALLIAIRSVSDKKEDG
RFTIFFNKREKKLSLHITDSQPGDSATYFCAASETGANTGKLTFGHGTILRVHPNIQNPD
PAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWS
NKSDFACANAFNNSIIPEDTFFPSPESS
Sequence of entity 4 (B), FASTA
>6MNO_4 6235 TCR beta chain (chains B)
AVTQSPRNKVAVTGGKVTLSCNQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIPD
GYKASRPSQENFSLILELATPSQTSVYFCASGDFWGDTLYFGAGTRLSVLEDLKNVFPPE
VAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPALN
DSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRA

Primary citation

A temporal thymic selection switch and ligand binding kinetics constrain neonatal Foxp3+Tregcell development. Stadinski, B.D., Blevins, S.J., Spidale, N.A. et al. Nat Immunol (2019) 20:1046-1058. DOI 10.1038/s41590-019-0414-1 · PubMed

Other PDB entries of the same protein (UniProt P14434 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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