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4G0A

Crystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of 5'-GG Sequence for RTPase activity

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0016787molecular_functionhydrolase activity
A0016817molecular_functionhydrolase activity, acting on acid anhydrides
A0017111molecular_functionribonucleoside triphosphate phosphatase activity
A0019079biological_processviral genome replication
A0030430cellular_componenthost cell cytoplasm
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005524molecular_functionATP binding
B0016787molecular_functionhydrolase activity
B0016817molecular_functionhydrolase activity, acting on acid anhydrides
B0017111molecular_functionribonucleoside triphosphate phosphatase activity
B0019079biological_processviral genome replication
B0030430cellular_componenthost cell cytoplasm
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0003723molecular_functionRNA binding
C0004550molecular_functionnucleoside diphosphate kinase activity
C0005524molecular_functionATP binding
C0016787molecular_functionhydrolase activity
C0016817molecular_functionhydrolase activity, acting on acid anhydrides
C0017111molecular_functionribonucleoside triphosphate phosphatase activity
C0019079biological_processviral genome replication
C0030430cellular_componenthost cell cytoplasm
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0003723molecular_functionRNA binding
D0004550molecular_functionnucleoside diphosphate kinase activity
D0005524molecular_functionATP binding
D0016787molecular_functionhydrolase activity
D0016817molecular_functionhydrolase activity, acting on acid anhydrides
D0017111molecular_functionribonucleoside triphosphate phosphatase activity
D0019079biological_processviral genome replication
D0030430cellular_componenthost cell cytoplasm
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 1201
ChainResidue
ATHR220
AHIS221
AGLY222
ALYS223
AHIS225
AARG227

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL B 1200
ChainResidue
BLYS223
BHIS225
BARG227
BTHR220
BHIS221
BGLY222

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL C 401
ChainResidue
CTHR220
CHIS221
CGLY222
CLYS223
CHIS225
CARG227

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA C 402
ChainResidue
CASP39
CLYS42
CPRO55
CHOH613

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL D 401
ChainResidue
DTHR220
DHIS221
DGLY222
DLYS223
DHIS225
DARG227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: For NTPase and RTPase activities => ECO:0000255|HAMAP-Rule:MF_04089, ECO:0000305|PubMed:17804496
ChainResidueDetails
AHIS225
BHIS225
CHIS225
DHIS225

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04089, ECO:0007744|PDB:2R7P
ChainResidueDetails
ASER107
CLYS188
CHIS221
CARG227
DSER107
DLYS188
DHIS221
DARG227
ALYS188
AHIS221
AARG227
BSER107
BLYS188
BHIS221
BARG227
CSER107

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PDB entries from 2025-06-18

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