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4YPT

X-ray structural of three tandemly linked domains of nsp3 from murine hepatitis virus at 2.60 Angstroms resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 2001
ChainResidue
ACYS1794
ACYS1796
ACYS1828
ACYS1830

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 2002
ChainResidue
AASP1643
AGLY1644
APHE1662
ATYR1689
ATYR1690

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 2003
ChainResidue
ASER1712
AASN1713
ASER1870
AVAL1871
AHIS1873

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 2004
ChainResidue
AARG1803
AHIS1811
APHE1812
ATYR1824
AILE1826

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL A 2005
ChainResidue
AGLY1785
AASN1841

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL A 2006
ChainResidue
ASER1761
AARG1779
AHOH2134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsZN_FING: C4-type 2 => ECO:0000255|PROSITE-ProRule:PRU00444
ChainResidueDetails
ACYS1794-CYS1830

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: For PL2-PRO activity => ECO:0000255|PROSITE-ProRule:PRU00444
ChainResidueDetails
AASP1887
AOCS1716
AHIS1873

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00444
ChainResidueDetails
ACYS1794
ACYS1796
ACYS1828
ACYS1830

221051

PDB entries from 2024-06-12

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