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2R8F

Crystal structure of H225A NSP2 and ATP-gS complex

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 318
ChainResidue
AARG210
ALYS301
AGLY302
ALEU303
ASER304
AHOH499

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AGS A 400
ChainResidue
ALYS223
AARG227
AARG240
ATHR244
AHOH412
AHOH413
AHOH416
AHOH490
AHOH494
AHOH495
AARG109
ALYS188
AHIS221

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For NTPase and RTPase activities => ECO:0000255|HAMAP-Rule:MF_04089, ECO:0000305|PubMed:17804496
ChainResidueDetails
AALA225

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04089, ECO:0007744|PDB:2R7P
ChainResidueDetails
ASER107
ALYS188
AHIS221
AARG227

219140

PDB entries from 2024-05-01

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