Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2O1C

Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase

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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 164
ChainResidue
ALYS4
ALYS7
AARG30
AARG90
AHOH190
AHOH253

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 165
ChainResidue
AARG97
AARG97
ATRP136
AHOH169
AHOH191
AHOH191
APHE81
AGLU82
AGLU82

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

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 B 163
ChainResidue
BPHE81
BGLU82
BARG97
BTRP136
BHOH169
CPHE81
CGLU82
CARG97
CTRP136
CHOH181
CHOH182

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PPV A 163
ChainResidue
ALYS7
AARG29
ATHR40
AGLY41
ASER42
AGLU56
AHOH194
AHOH198
AHOH238
AHOH282

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PPV B 165
ChainResidue
BLYS7
BARG29
BTHR40
BGLY41
BSER42
BGLU56
BHOH209
BHOH315

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PPV C 163
ChainResidue
CLYS7
CTHR40
CGLY41
CSER42
CGLU56
CARG90
CHOH177
CHOH245
CHOH272
CHOH274

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 Residues24
DetailsBINDING:
ChainResidueDetails
CLYS7
CARG29
CTHR40
CGLU56
CGLU60
CGLU117
DLYS7
DARG29
DTHR40
DGLU56
DGLU60
DGLU117
ALYS7
AARG29
ATHR40
AGLU56
AGLU60
AGLU117
BLYS7
BARG29
BTHR40
BGLU56
BGLU60
BGLU117

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
APHE81
ASER135
BPHE81
BSER135
CPHE81
CSER135
DPHE81
DSER135

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon