Anti citrullinated Collagen type 2 antibody acc4. Determined by X-ray diffraction at 1.5 Å resolution. Released 24 Feb 2009.
Explore 2W60 in 3D Show helices and sheets RCSB PDB PDBe
2W60 contains 17 α-helices and 45 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 46-51 | 6 | 2 |
| β-strand | 58-60 | 3 | 2 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 1 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 2 |
| β-strand | 107-108 | 2 | 2 |
| β-strand | 112-116 | 5 | 2 |
| β-strand | 122 | 1 | 3 |
| α-helix | 123-124 | 2 | |
| β-strand | 125-129 | 5 | 4 |
| β-strand | 140-150 | 11 | 4 |
| β-strand | 151 | 1 | 3 |
| β-strand | 156-159 | 4 | 5 |
| α-helix | 160-162 | 3 | |
| β-strand | 164 | 1 | 5 |
| β-strand | 168-170 | 3 | 4 |
| α-helix | 171-173 | 3 | |
| β-strand | 174-175 | 2 | 4 |
| β-strand | 180-189 | 10 | 4 |
| β-strand | 199-204 | 6 | 5 |
| α-helix | 205-207 | 3 | |
| β-strand | 209-214 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-13 | 4 | 7 |
| β-strand | 19-25 | 7 | 6 |
| β-strand | 30 | 1 | 8 |
| β-strand | 36 | 1 | 8 |
| β-strand | 38-43 | 6 | 7 |
| β-strand | 50-54 | 5 | 7 |
| β-strand | 58-59 | 2 | 7 |
| α-helix | 60 | 1 | |
| β-strand | 67-72 | 6 | 6 |
| β-strand | 75-80 | 6 | 6 |
| α-helix | 85-87 | 3 | |
| β-strand | 89-95 | 7 | 7 |
| α-helix | 101 | 1 | |
| β-strand | 102-103 | 2 | 7 |
| β-strand | 107-111 | 5 | 7 |
| β-strand | 116 | 1 | 9 |
| α-helix | 117-118 | 2 | |
| β-strand | 119-123 | 5 | 10 |
| α-helix | 124-126 | 3 | |
| α-helix | 127-131 | 5 | |
| β-strand | 134-144 | 11 | 10 |
| β-strand | 145 | 1 | 9 |
| β-strand | 150-155 | 6 | 11 |
| β-strand | 158-159 | 2 | 11 |
| β-strand | 163-168 | 6 | 10 |
| α-helix | 169-172 | 4 | |
| β-strand | 178-187 | 10 | 10 |
| α-helix | 188-191 | 4 | |
| β-strand | 196-202 | 7 | 11 |
| α-helix | 209 | 1 | |
| β-strand | 210-215 | 6 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Anti-citrullinated collagen type II FAB ACC4 | A | protein | 218 | MUS MUSCULUS | |
| Anti-citrullinated collagen type II FAB ACC4 | B | protein | 217 | MUS MUSCULUS | P01837 (AlphaFold model) |
>2W60_1 ANTI-CITRULLINATED COLLAGEN TYPE II FAB ACC4 (chains A) QIQLVQSGPELKKPGETVKISCKASGYTFTDYSIHWVKQAPGKGLKWMGWINTETGEPTY TDDFKGRFAFSLESSASTAFLQINNLKNEDTATYFCARATTATELAYWGQGTLVTVSAAK TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY TLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPR
>2W60_2 ANTI-CITRULLINATED COLLAGEN TYPE II FAB ACC4 (chains B) DVVMTQTPLTLSVTIGQPASISCKSSQSLLDSDGKTYLNWLLQRPGQSPKRLIYLVSKLD SGVPDRFTGSGSGTDFTLKISRVEAEDLGVYYCWQGTHFPLTFGAGTKLELKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRN
Structure and pathogenicity of antibodies specific for citrullinated collagen type II in experimental arthritis. Uysal, H., Bockermann, R., Nandakumar, K.S. et al. J Exp Med (2009) 206:449-462. DOI 10.1084/jem.20081862 · PubMed
Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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