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2O5W

Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase in complex with Sm+3 and pyrophosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0008828molecular_functiondATP diphosphatase activity
A0016787molecular_functionhydrolase activity
A0019177molecular_functiondihydroneopterin triphosphate pyrophosphohydrolase activity
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0008828molecular_functiondATP diphosphatase activity
B0016787molecular_functionhydrolase activity
B0019177molecular_functiondihydroneopterin triphosphate pyrophosphohydrolase activity
B0046654biological_processtetrahydrofolate biosynthetic process
B0046656biological_processfolic acid biosynthetic process
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0008828molecular_functiondATP diphosphatase activity
C0016787molecular_functionhydrolase activity
C0019177molecular_functiondihydroneopterin triphosphate pyrophosphohydrolase activity
C0046654biological_processtetrahydrofolate biosynthetic process
C0046656biological_processfolic acid biosynthetic process
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0008828molecular_functiondATP diphosphatase activity
D0016787molecular_functionhydrolase activity
D0019177molecular_functiondihydroneopterin triphosphate pyrophosphohydrolase activity
D0046654biological_processtetrahydrofolate biosynthetic process
D0046656biological_processfolic acid biosynthetic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 164
ChainResidue
ALYS4
ALYS7
AARG90
APPV163

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 165
ChainResidue
AARG97
AARG97
ATRP136
ATRP136
AHOH192
AGLU80
APHE81
APHE81
AGLU82
AGLU82

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 164
ChainResidue
BLYS4
BLYS7
BARG90

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 165
ChainResidue
BPHE81
BGLU82
BARG97
BTRP136
CPHE81
CGLU82
CARG97
CTRP136

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SM A 170
ChainResidue
AGLU56
AGLU59
AGLU117
APPV163
ANA171

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SM B 170
ChainResidue
BGLU56
BGLU59
BGLU60
BGLU117

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SM C 170
ChainResidue
CGLU56
CGLU59
CGLU117
CPPV163
CNA171

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 171
ChainResidue
ATHR40
AGLU56
AGLU60
APPV163
ASM170

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA C 171
ChainResidue
CTHR40
CGLU56
CGLU60
CGLU117
CPPV163
CSM170

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PPV A 163
ChainResidue
ALYS7
AARG29
ATHR40
AGLY41
ASO4164
ASM170
ANA171

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PPV C 163
ChainResidue
CLYS7
CARG29
CTHR40
CGLY41
CSM170
CNA171
CHOH183

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GsveegEtapqAAmREVkEEvT
ChainResidueDetails
AGLY41-THR62

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues282
DetailsDomain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues84
DetailsMotif: {"description":"Nudix box"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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