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5WWD

Crystal structure of AtNUDX1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000210molecular_functionNAD+ diphosphatase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006974biological_processDNA damage response
A0008413molecular_function8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
A0016787molecular_functionhydrolase activity
A0019177molecular_functiondihydroneopterin triphosphate pyrophosphohydrolase activity
A0035529molecular_functionNADH pyrophosphatase activity
A0035539molecular_function8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity
A0046872molecular_functionmetal ion binding
B0000210molecular_functionNAD+ diphosphatase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006974biological_processDNA damage response
B0008413molecular_function8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
B0016787molecular_functionhydrolase activity
B0019177molecular_functiondihydroneopterin triphosphate pyrophosphohydrolase activity
B0035529molecular_functionNADH pyrophosphatase activity
B0035539molecular_function8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GOL A 201
ChainResidue
AASN105
AGLY113
ATRP114
AHOH303
AHOH379
BLYS104
BASN105
BHOH347

site_idAC2
Number of Residues5
Detailsbinding site for residue 2ME A 202
ChainResidue
AVAL77
ATRP128
ALYS132
AHOH333
AASN75

site_idAC3
Number of Residues1
Detailsbinding site for residue NH4 A 203
ChainResidue
ASER89

site_idAC4
Number of Residues4
Detailsbinding site for residue MG A 204
ChainResidue
AGLY41
AHIS42
AMG205
AHOH342

site_idAC5
Number of Residues6
Detailsbinding site for residue MG A 205
ChainResidue
AGLU56
AMG204
AMG206
AHOH302
AHOH342
AHOH365

site_idAC6
Number of Residues6
Detailsbinding site for residue MG A 206
ChainResidue
AGLU56
AGLU59
AGLU60
AGLU107
AMG205
AHOH342

site_idAC7
Number of Residues8
Detailsbinding site for residue GOL B 201
ChainResidue
AASN20
ATRP119
AGLU120
AASN139
APHE141
BTRP119
BGLU120
BGOL203

site_idAC8
Number of Residues9
Detailsbinding site for residue GOL B 202
ChainResidue
BARG28
BSER34
BGLU112
BHOH302
BHOH315
BHOH322
BHOH346
BHOH407
BHOH417

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL B 203
ChainResidue
ATRP119
AGLU120
BASN20
BTRP119
BASN139
BPHE141
BGOL201

site_idAD1
Number of Residues3
Detailsbinding site for residue MG B 204
ChainResidue
BGLU56
BMG205
BHOH363

site_idAD2
Number of Residues3
Detailsbinding site for residue MG B 205
ChainResidue
BGLY41
BHIS42
BMG204

site_idAD3
Number of Residues4
Detailsbinding site for residue MG B 206
ChainResidue
BGLU56
BGLU59
BGLU107
BLYS110

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GhlefgEsfeeCAaREVmEEtG
ChainResidueDetails
AGLY41-GLY62

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU56
AGLU60
BGLU56
BGLU60

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22223895
ChainResidueDetails
ASER2
BSER2

226707

PDB entries from 2024-10-30

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