1ZGL: 3A6 TCR
Crystal structure of 3A6 TCR bound to MBP/HLA-DR2a. Determined by X-ray diffraction at 2.8 Å resolution. Released 18 Oct 2005.
- Method
- X-ray diffraction
- Resolution
- 2.8 Å
- Organism
- Homo sapiens
- Chains
- 20
- Atoms
- 23,456
- Mol. weight
- 383.73 kDa
- Released
- 18 Oct 2005
Explore 1ZGL in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1ZGL contains 57 α-helices and 295 β-strands across 19 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: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-15 | 11 | 1 |
| β-strand | 19-26 | 8 | 1 |
| β-strand | 29-35 | 7 | 1 |
| β-strand | 40-43 | 4 | 1 |
| α-helix | 48-50 | 3 | |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 59-76 | 18 | |
| α-helix | 80-82 | 3 | |
| β-strand | 85 | 1 | 3 |
| β-strand | 88-93 | 6 | 4 |
| β-strand | 103-112 | 10 | 4 |
| β-strand | 113 | 1 | 3 |
| β-strand | 118-122 | 5 | 5 |
| β-strand | 127-128 | 2 | 5 |
| β-strand | 133-134 | 2 | 4 |
| β-strand | 145-153 | 9 | 4 |
| β-strand | 161-166 | 6 | 5 |
| β-strand | 174-178 | 5 | 5 |
Chain B: 7 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-18 | 12 | 1 |
| β-strand | 23-32 | 10 | 1 |
| β-strand | 35-41 | 7 | 1 |
| α-helix | 42-44 | 3 | |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-62 | 8 | |
| α-helix | 67-72 | 6 | |
| α-helix | 74 | 1 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-87 | 7 | |
| β-strand | 95 | 1 | 6 |
| β-strand | 100-102 | 3 | 7 |
| β-strand | 116-120 | 5 | 7 |
| β-strand | 123 | 1 | 6 |
| β-strand | 128-130 | 3 | 8 |
| β-strand | 144 | 1 | 7 |
| β-strand | 148-149 | 2 | 7 |
| β-strand | 155-160 | 6 | 7 |
| β-strand | 172-176 | 5 | 8 |
| β-strand | 184-187 | 4 | 8 |
Chain C: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-4 | 2 | 2 |
| α-helix | 5 | 1 | |
Chain D: 2 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-15 | 11 | 22 |
| β-strand | 19-26 | 8 | 22 |
| β-strand | 29-35 | 7 | 22 |
| β-strand | 40-43 | 4 | 22 |
| α-helix | 46-50 | 5 | |
| β-strand | 53 | 1 | 23 |
| α-helix | 59-77 | 19 | |
| β-strand | 85 | 1 | 24 |
| β-strand | 88-93 | 6 | 25 |
| β-strand | 103-112 | 10 | 25 |
| β-strand | 113 | 1 | 24 |
| β-strand | 118-123 | 6 | 26 |
| β-strand | 126-127 | 2 | 26 |
| β-strand | 133-139 | 7 | 25 |
| β-strand | 145-153 | 9 | 25 |
| β-strand | 161-166 | 6 | 26 |
| β-strand | 174-178 | 5 | 26 |
Chain E: 7 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-18 | 12 | 22 |
| β-strand | 23-32 | 10 | 22 |
| β-strand | 35-41 | 7 | 22 |
| α-helix | 42-44 | 3 | |
| β-strand | 46-48 | 3 | 22 |
| α-helix | 55-61 | 7 | |
| α-helix | 67-72 | 6 | |
| α-helix | 74 | 1 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-87 | 7 | |
| β-strand | 95 | 1 | 27 |
| α-helix | 96-97 | 2 | |
| β-strand | 100-102 | 3 | 28 |
| β-strand | 115-122 | 8 | 28 |
| β-strand | 123 | 1 | 27 |
| β-strand | 129-130 | 2 | 29 |
| β-strand | 144 | 1 | 28 |
| β-strand | 148-149 | 2 | 28 |
| β-strand | 155-161 | 7 | 28 |
| β-strand | 171-172 | 2 | 30 |
| β-strand | 174-175 | 2 | 29 |
| β-strand | 184 | 1 | 29 |
| β-strand | 187-188 | 2 | 30 |
Chain F: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 23 |
Chain G: 3 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-15 | 11 | 44 |
| β-strand | 19-26 | 8 | 44 |
| β-strand | 29-34 | 6 | 44 |
| β-strand | 41-43 | 3 | 44 |
| α-helix | 46-50 | 5 | |
| α-helix | 59-76 | 18 | |
| β-strand | 85 | 1 | 45 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-93 | 6 | 46 |
| β-strand | 103-112 | 10 | 46 |
| β-strand | 113 | 1 | 45 |
| β-strand | 118-123 | 6 | 47 |
| β-strand | 126-128 | 3 | 47 |
| β-strand | 133-134 | 2 | 46 |
| β-strand | 138-139 | 2 | 46 |
| β-strand | 145-153 | 9 | 46 |
| β-strand | 161-166 | 6 | 47 |
| β-strand | 174 | 1 | 47 |
| β-strand | 177-178 | 2 | 47 |
Chain H: 7 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-18 | 12 | 44 |
| β-strand | 23-32 | 10 | 44 |
| β-strand | 35-41 | 7 | 44 |
| α-helix | 42-44 | 3 | |
| β-strand | 46-48 | 3 | 44 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-61 | 7 | |
| α-helix | 66-72 | 7 | |
| α-helix | 74 | 1 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-87 | 7 | |
| β-strand | 95 | 1 | 48 |
| β-strand | 99-103 | 5 | 49 |
| β-strand | 115-122 | 8 | 49 |
| β-strand | 123 | 1 | 48 |
| β-strand | 128-131 | 4 | 50 |
| β-strand | 148-149 | 2 | 49 |
| β-strand | 155-161 | 7 | 49 |
| β-strand | 173-176 | 4 | 50 |
| β-strand | 184 | 1 | 50 |
11 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| HLA class II histocompatibility antigen, DR alpha chain | A, D, G, J | protein | 181 | Homo sapiens | P01903 (AlphaFold model) |
| major histocompatibility complex, class II, DR beta 5 | B, E, H, K | protein | 192 | Homo sapiens | Q30154 (AlphaFold model) |
| Myelin basic protein | C, F, I, L | protein | 15 | Homo sapiens | P02686 (AlphaFold model) |
| T cell receptor alpha chain | M, Q, S, U | protein | 209 | Homo sapiens | P01848 (AlphaFold model) |
| T cell receptor beta chain | P, R, T, V | protein | 249 | Homo sapiens | P01850 |
Sequence of entity 1 (A, D, G, J), FASTA
>1ZGL_1 HLA class II histocompatibility antigen, DR alpha chain (chains A, D, G, J)
IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGAL
ANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVT
WLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEF
D
Sequence of entity 2 (B, E, H, K), FASTA
>1ZGL_2 major histocompatibility complex, class II, DR beta 5 (chains B, E, H, K)
GDTRPRFLQQDKYECHFFNGTERVRFLHRDIYNQEEDLRFDSDVGEYRAVTELGRPDAEY
WNSQKDFLEDRRAAVDTYCRHNYGVGESFTVQRRVEPKVTVYPARTQTLQHHNLLVCSVN
GFYPGSIEVRWFRNSQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSV
TSPLTVEWRAQS
Sequence of entity 3 (C, F, I, L), FASTA
>1ZGL_3 Myelin basic protein (chains C, F, I, L)
VHFFKNIVTPRTPGG
Sequence of entity 4 (M, Q, S, U), FASTA
>1ZGL_4 T cell receptor alpha chain (chains M, Q, S, U)
GDSVTQMEGPVTLSEEAFLTINCTYTATGYPSLFWYVQYPGEGLQLLLKATKADDKGSNK
GFEATYRKETTSFHLEKGSVQVSDSAVYFCALSGGDSSYKLIFGSGTRLLVRPDIQNPDP
AVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSN
KSDFACANAFNNSIIPEDTFFPSPESSCA
Sequence of entity 5 (P, R, T, V), FASTA
>1ZGL_5 T cell receptor beta chain (chains P, R, T, V)
GGGGGVTQTPRYLIKTRGQQVTLSCSPISGHRSVSWYQQTPGQGLQFLFEYFNETQRNKG
NFPGRFSGRQFSNSRSEMNVSTLELGDSALYLCASSLADRVNTEAFFGQGTRLTVVEDLK
NVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLK
EQPALNDSRYSLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAE
AWGRADCAA
Primary citation
Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule. Li, Y., Huang, Y., Lue, J. et al. EMBO J (2005) 24:2968-2979. DOI 10.1038/sj.emboj.7600771 · PubMed
Other PDB entries of the same protein (UniProt P01903 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5NI9 1.33 Å, Crystal structure of HLA-DRB1*04:01 with the alpha-enolase peptide 326-340
- 4X5W 1.34 Å, HLA-DR1 with CLIP102-120(M107W)
- 5NIG 1.35 Å, Crystal structure of HLA-DRB1*04:01 with modified alpha-enolase peptide 326-340…
- 8CMC 1.42 Å, Human Leukocyte Antigen class II allotype DR1 presenting SARS-CoV-2 Spike peptide S511-530
- 8PJF 1.48 Å, Human Leukocyte Antigen class II allotype DR1 presenting P11T->R modified influenza A…
- 6QZC 1.64 Å, HLA-DR1 with the QAR Peptide
- 8CMG 1.64 Å, Human Leukocyte Antigen class II allotype DR1 presenting SARS-CoV-2 nsp14 peptide…
- 8CMH 1.64 Å, Human Leukocyte Antigen class II allotype DR1 presenting SARS-CoV-2 Omicron (BA.1) Spike…
- 4MD5 1.65 Å, Immune Receptor
- 4MDJ 1.7 Å, Immune Receptor
- 8PJE 1.7 Å, Human Leukocyte Antigen class II allotype DR1 presenting influenza A virus…
- 7YX9 1.76 Å, MHC-II dynamics are maintained in HLA-DR allotypes to ensure catalyzed peptide exchange
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