2FSE: PDB entry 2FSE
Crystallographic structure of a rheumatoid arthritis MHC susceptibility allele, HLA-DR1 (DRB1*0101), complexed with the immunodominant determinant of human type II collagen. Determined by X-ray diffraction at 3.1 Å resolution. Released 19 Sept 2006.
- Method
- X-ray diffraction
- Resolution
- 3.1 Å
- Organisms
- Homo sapiens, Mus musculus
- Chains
- 6
- Atoms
- 6,216
- Mol. weight
- 87.96 kDa
- Released
- 19 Sept 2006
Explore 2FSE in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2FSE contains 21 α-helices and 59 β-strands across 6 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, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-15 | 10 | 1 |
| β-strand | 19-26 | 8 | 1 |
| β-strand | 29-35 | 7 | 1 |
| β-strand | 40-43 | 4 | 1 |
| α-helix | 46-51 | 6 | |
| α-helix | 57-75 | 19 | |
| β-strand | 85 | 1 | 2 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-93 | 6 | 3 |
| β-strand | 103-112 | 10 | 3 |
| β-strand | 113 | 1 | 2 |
| β-strand | 118-123 | 6 | 4 |
| β-strand | 126-127 | 2 | 4 |
| α-helix | 128 | 1 | |
| β-strand | 132-134 | 3 | 3 |
| β-strand | 138-139 | 2 | 3 |
| β-strand | 145-153 | 9 | 3 |
| β-strand | 161-166 | 6 | 4 |
| β-strand | 174-178 | 5 | 4 |
Chain B: 6 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-18 | 12 | 1 |
| β-strand | 23-31 | 9 | 1 |
| β-strand | 36-41 | 6 | 1 |
| β-strand | 46-49 | 4 | 1 |
| α-helix | 55-63 | 9 | |
| α-helix | 65-74 | 10 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-86 | 6 | |
| α-helix | 87-89 | 3 | |
| β-strand | 95 | 1 | 5 |
| α-helix | 96-97 | 2 | |
| β-strand | 98-103 | 6 | 6 |
| β-strand | 113-122 | 10 | 6 |
| β-strand | 123 | 1 | 5 |
| β-strand | 128-133 | 6 | 7 |
| β-strand | 136-137 | 2 | 7 |
| β-strand | 140 | 1 | 6 |
| β-strand | 142-149 | 8 | 6 |
| β-strand | 155-163 | 9 | 6 |
| β-strand | 170-176 | 7 | 7 |
| β-strand | 184-189 | 6 | 7 |
Chain C: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-15 | 11 | 8 |
| β-strand | 19-26 | 8 | 8 |
| β-strand | 29-35 | 7 | 8 |
| β-strand | 40-43 | 4 | 8 |
| α-helix | 46-49 | 4 | |
| α-helix | 56-76 | 21 | |
| α-helix | 80-84 | 5 | |
| β-strand | 85 | 1 | 9 |
| β-strand | 88-93 | 6 | 10 |
| β-strand | 103-112 | 10 | 10 |
| β-strand | 113 | 1 | 9 |
| β-strand | 118-123 | 6 | 11 |
| β-strand | 126-127 | 2 | 11 |
| β-strand | 132-134 | 3 | 10 |
| β-strand | 138-139 | 2 | 10 |
| β-strand | 145-153 | 9 | 10 |
| β-strand | 161-166 | 6 | 11 |
| β-strand | 174-178 | 5 | 11 |
Chain D: 6 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-18 | 12 | 8 |
| β-strand | 23-31 | 9 | 8 |
| β-strand | 36-41 | 6 | 8 |
| β-strand | 47 | 1 | 8 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-63 | 9 | |
| α-helix | 65-74 | 10 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-86 | 6 | |
| α-helix | 87-89 | 3 | |
| β-strand | 95 | 1 | 12 |
| β-strand | 98-102 | 5 | 6 |
| β-strand | 113-122 | 10 | 6 |
| β-strand | 123 | 1 | 12 |
| β-strand | 128-133 | 6 | 13 |
| β-strand | 136-137 | 2 | 13 |
| β-strand | 143-149 | 7 | 6 |
| β-strand | 155-163 | 9 | 6 |
| β-strand | 171-176 | 6 | 13 |
| β-strand | 184-188 | 5 | 13 |
Chain E: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1009-1011 | 3 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2002-2005 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| H-2 class II histocompatibility antigen, E-K alpha chain | A, C | protein | 178 | Homo sapiens | P01903 (AlphaFold model) |
| HLA class II histocompatibility antigen, DRB1-1 beta chain | B, D | protein | 187 | Mus musculus | P01911 (AlphaFold model) |
| Collagen alpha-1(II) | E, F | protein | 14 | Homo sapiens | P02458 (AlphaFold model) |
Sequence of entity 1 (A, C), FASTA
>2FSE_1 H-2 class II histocompatibility antigen, E-K alpha chain (chains A, C)
EHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANI
AVDKANLEIMTKRSNYTPITNVAPEVTVLSRSPVNLGEPNILICFIDKFSPPVVNVTWLR
NGRPVTEGVSETVFLPRDDHLFRKFHYLTFLPSTDDFYDCEVDHWGLEEPLRKHWEFE
Sequence of entity 2 (B, D), FASTA
>2FSE_2 HLA class II histocompatibility antigen, DRB1-1 beta chain (chains B, D)
RPRFLWQLKFECHFFNGTERVRLLERCIYNQEESVRFDSDVGEYRAVTELGRPDAEYWNS
QKDLLEQRRAAVDTYCRHNYGVGESFTVQRRVEPTVTVYPTKTQPLQHHNLLVCSVSDFY
PGNIEVRWFRNGKEEETGIVSTGLVRNGDWTFQTLVMLETVPQSGEVYTCQVEHPSLTDP
VTVEWKA
Sequence of entity 3 (E, F), FASTA
>2FSE_3 Collagen alpha-1(II) (chains E, F)
AGFKGEQGPKGEPG
Primary citation
Crystallographic Structure of a Rheumatoid Arthritis MHC Susceptibility Allele, HLA-DR1 (DRB1*0101), Complexed with the Immunodominant Determinant of Human Type II Collagen. Rosloniec, E.F., Ivey, R.A., Whittington, K.B. et al. J Immunol (2006) 177:3884-3892. 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
Browse structure collections
About this viewer
MolViewer shows 2FSE 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.