NSP4 proteinase from Equine Arteritis Virus. Determined by X-ray diffraction at 2.0 Å resolution. Released 23 Oct 2002.
Explore 1MBM in 3D Show helices and sheets RCSB PDB PDBe
1MBM contains 29 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-16 | 5 | 1 |
| β-strand | 20-28 | 9 | 1 |
| β-strand | 31-37 | 7 | 1 |
| α-helix | 38-41 | 4 | |
| β-strand | 46-51 | 6 | 1 |
| β-strand | 54-59 | 6 | 1 |
| β-strand | 61-63 | 3 | 1 |
| β-strand | 66-71 | 6 | 1 |
| α-helix | 80-81 | 2 | |
| β-strand | 82 | 1 | 1 |
| α-helix | 83 | 1 | |
| β-strand | 85 | 1 | 2 |
| β-strand | 91-98 | 8 | 2 |
| β-strand | 100-106 | 7 | 2 |
| β-strand | 111-112 | 2 | 2 |
| α-helix | 117-119 | 3 | |
| β-strand | 123-126 | 4 | 2 |
| β-strand | 129-138 | 10 | 2 |
| α-helix | 139-141 | 3 | |
| β-strand | 142-146 | 5 | 2 |
| α-helix | 151 | 1 | |
| β-strand | 152-153 | 2 | 2 |
| β-strand | 158-159 | 2 | 3 |
| α-helix | 160-164 | 5 | |
| β-strand | 171-173 | 3 | 4 |
| α-helix | 174-175 | 2 | |
| β-strand | 182-183 | 2 | 3 |
| β-strand | 188-190 | 3 | 4 |
| α-helix | 191-198 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-16 | 5 | 5 |
| β-strand | 20-27 | 8 | 5 |
| β-strand | 32-37 | 6 | 5 |
| α-helix | 38-41 | 4 | |
| β-strand | 46-51 | 6 | 5 |
| β-strand | 54-63 | 10 | 5 |
| β-strand | 66-71 | 6 | 5 |
| α-helix | 80-81 | 2 | |
| β-strand | 82 | 1 | 5 |
| α-helix | 83 | 1 | |
| β-strand | 85 | 1 | 6 |
| β-strand | 91-97 | 7 | 6 |
| β-strand | 100-106 | 7 | 6 |
| β-strand | 111-112 | 2 | 6 |
| β-strand | 123-126 | 4 | 6 |
| β-strand | 129-138 | 10 | 6 |
| β-strand | 142-146 | 5 | 6 |
| β-strand | 152-153 | 2 | 6 |
| β-strand | 158-159 | 2 | 7 |
| α-helix | 160-164 | 5 | |
| β-strand | 171-173 | 3 | 8 |
| α-helix | 174-175 | 2 | |
| β-strand | 182-183 | 2 | 7 |
| β-strand | 188-190 | 3 | 8 |
| α-helix | 191-196 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-16 | 5 | 9 |
| β-strand | 20-27 | 8 | 9 |
| β-strand | 32-37 | 6 | 9 |
| α-helix | 38-41 | 4 | |
| β-strand | 46-51 | 6 | 9 |
| β-strand | 54-59 | 6 | 9 |
| β-strand | 61-63 | 3 | 9 |
| β-strand | 66-71 | 6 | 9 |
| α-helix | 80-81 | 2 | |
| β-strand | 82 | 1 | 9 |
| α-helix | 83 | 1 | |
| β-strand | 85 | 1 | 10 |
| β-strand | 91-97 | 7 | 10 |
| β-strand | 100-106 | 7 | 10 |
| β-strand | 111-112 | 2 | 10 |
| α-helix | 117-119 | 3 | |
| β-strand | 123-126 | 4 | 10 |
| β-strand | 129-138 | 10 | 10 |
| β-strand | 142-146 | 5 | 10 |
| β-strand | 152-153 | 2 | 10 |
| β-strand | 158-159 | 2 | 11 |
| α-helix | 160-164 | 5 | |
| β-strand | 171-173 | 3 | 12 |
| α-helix | 174-175 | 2 | |
| β-strand | 182-183 | 2 | 11 |
| β-strand | 188-190 | 3 | 12 |
| α-helix | 191-196 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-16 | 5 | 13 |
| β-strand | 20-28 | 9 | 13 |
| β-strand | 31-37 | 7 | 13 |
| α-helix | 38-41 | 4 | |
| β-strand | 46-51 | 6 | 13 |
| β-strand | 54-59 | 6 | 13 |
| β-strand | 61-63 | 3 | 13 |
| β-strand | 66-71 | 6 | 13 |
| α-helix | 80-81 | 2 | |
| β-strand | 82 | 1 | 13 |
| α-helix | 83 | 1 | |
| β-strand | 85 | 1 | 14 |
| β-strand | 91-97 | 7 | 14 |
| β-strand | 100-106 | 7 | 14 |
| β-strand | 111-112 | 2 | 14 |
| α-helix | 117-119 | 3 | |
| β-strand | 123-126 | 4 | 14 |
| β-strand | 129-138 | 10 | 14 |
| β-strand | 142-146 | 5 | 14 |
| β-strand | 152-153 | 2 | 14 |
| β-strand | 158-159 | 2 | 15 |
| α-helix | 160-164 | 5 | |
| β-strand | 171-173 | 3 | 16 |
| α-helix | 174-175 | 2 | |
| β-strand | 182-183 | 2 | 15 |
| β-strand | 188-190 | 3 | 16 |
| α-helix | 191-197 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| chymotrypsin-like serine protease | A, B, C, D | protein | 198 | Equine arteritis virus | P19811 (AlphaFold model) |
>1MBM_1 chymotrypsin-like serine protease (chains A, B, C, D) KARGNVGFVAGSSYGTGSVWTRNNEVVVLTASHVVGRANMATLKIGDAMLTLTFKKNGDF AEAVTTQSELPGNWPQLHFAQPTTGPASWCTATGDEEGLLSGEVCLAWTTSGDSGSAVVQ GDAVVGVHTGSNTSGVAYVTTPSGKLLGADTVTLSSLSKHFTGPLTSIPKDIPDNIIADV DAVPRSLAMLIDGLSNRE
Structure of Arterivirus nsp4: the smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole. Barrette-Ng, I.H., Ng, K.K.-S., Mark, B.L. et al. J Biol Chem (2002) 277:39960-39966. DOI 10.1074/jbc.M206978200 · PubMed
Other PDB entries of the same protein (UniProt P19811 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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