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4UON

Crystal structure of C-terminal truncated (110-265) Aura virus capsid protease.

Replaces:  4AUS
Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 1262
ChainResidue
AHIS-1

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1263
ChainResidue
AGLY147
ATHR148
AILE149
APHE159
AGLU168
AHOH2081

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1264
ChainResidue
AASP217
ASER218
AGLY235
ALEU245
AHOH2227
AGLY213
AGLY214

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1262
ChainResidue
BGLY147
BTHR148
BILE149
BALA155
BPHE159
BGLU168
BHOH2056
BHOH2172

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1263
ChainResidue
BTYR131
BHIS196
BGLY213
BGLY214
BGLY216
BASP217
BARG220

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1264
ChainResidue
BTRP194
BGLY214
BASP217
BSER218
BGLY236
BHOH2136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027
ChainResidueDetails
AHIS144
AASP166
ASER218
BHIS144
BASP166
BSER218

site_idSWS_FT_FI2
Number of Residues6
DetailsSITE: Involved in dimerization of the capsid protein => ECO:0000269|PubMed:25100849
ChainResidueDetails
APHE191
ATYR192
AASN225
BPHE191
BTYR192
BASN225

222036

PDB entries from 2024-07-03

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