1MBM: NSP4 proteinase from Equine Arteritis Virus

NSP4 proteinase from Equine Arteritis Virus. Determined by X-ray diffraction at 2.0 Å resolution. Released 23 Oct 2002.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Equine arteritis virus
Chains
4
Atoms
5,997
Mol. weight
81.51 kDa
Released
23 Oct 2002

Explore 1MBM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 9 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand12-1651
β-strand20-2891
β-strand31-3771
α-helix38-414
β-strand46-5161
β-strand54-5961
β-strand61-6331
β-strand66-7161
α-helix80-812
β-strand8211
α-helix831
β-strand8512
β-strand91-9882
β-strand100-10672
β-strand111-11222
α-helix117-1193
β-strand123-12642
β-strand129-138102
α-helix139-1413
β-strand142-14652
α-helix1511
β-strand152-15322
β-strand158-15923
α-helix160-1645
β-strand171-17334
α-helix174-1752
β-strand182-18323
β-strand188-19034
α-helix191-1988
Chain B: 6 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand12-1655
β-strand20-2785
β-strand32-3765
α-helix38-414
β-strand46-5165
β-strand54-63105
β-strand66-7165
α-helix80-812
β-strand8215
α-helix831
β-strand8516
β-strand91-9776
β-strand100-10676
β-strand111-11226
β-strand123-12646
β-strand129-138106
β-strand142-14656
β-strand152-15326
β-strand158-15927
α-helix160-1645
β-strand171-17338
α-helix174-1752
β-strand182-18327
β-strand188-19038
α-helix191-1966
Chain C: 7 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand12-1659
β-strand20-2789
β-strand32-3769
α-helix38-414
β-strand46-5169
β-strand54-5969
β-strand61-6339
β-strand66-7169
α-helix80-812
β-strand8219
α-helix831
β-strand85110
β-strand91-97710
β-strand100-106710
β-strand111-112210
α-helix117-1193
β-strand123-126410
β-strand129-1381010
β-strand142-146510
β-strand152-153210
β-strand158-159211
α-helix160-1645
β-strand171-173312
α-helix174-1752
β-strand182-183211
β-strand188-190312
α-helix191-1966
Chain D: 7 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand12-16513
β-strand20-28913
β-strand31-37713
α-helix38-414
β-strand46-51613
β-strand54-59613
β-strand61-63313
β-strand66-71613
α-helix80-812
β-strand82113
α-helix831
β-strand85114
β-strand91-97714
β-strand100-106714
β-strand111-112214
α-helix117-1193
β-strand123-126414
β-strand129-1381014
β-strand142-146514
β-strand152-153214
β-strand158-159215
α-helix160-1645
β-strand171-173316
α-helix174-1752
β-strand182-183215
β-strand188-190316
α-helix191-1977

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
chymotrypsin-like serine proteaseA, B, C, Dprotein198Equine arteritis virusP19811 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>1MBM_1 chymotrypsin-like serine protease (chains A, B, C, D)
KARGNVGFVAGSSYGTGSVWTRNNEVVVLTASHVVGRANMATLKIGDAMLTLTFKKNGDF
AEAVTTQSELPGNWPQLHFAQPTTGPASWCTATGDEEGLLSGEVCLAWTTSGDSGSAVVQ
GDAVVGVHTGSNTSGVAYVTTPSGKLLGADTVTLSSLSKHFTGPLTSIPKDIPDNIIADV
DAVPRSLAMLIDGLSNRE

Primary citation

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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