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2FVV

Human Diphosphoinositol polyphosphate phosphohydrolase 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000298molecular_functionendopolyphosphatase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007267biological_processcell-cell signaling
A0008270molecular_functionzinc ion binding
A0008486molecular_functiondiphosphoinositol-polyphosphate diphosphatase activity
A0015961biological_processdiadenosine polyphosphate catabolic process
A0016462molecular_functionpyrophosphatase activity
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0034431molecular_functionbis(5'-adenosyl)-hexaphosphatase activity
A0034432molecular_functionbis(5'-adenosyl)-pentaphosphatase activity
A0046872molecular_functionmetal ion binding
A0052840molecular_functioninositol diphosphate tetrakisphosphate diphosphatase activity
A0052842molecular_functioninositol diphosphate pentakisphosphate diphosphatase activity
A0052845molecular_functioninositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity
A0052848molecular_functioninositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity
A0071543biological_processdiphosphoinositol polyphosphate metabolic process
A0071544biological_processdiphosphoinositol polyphosphate catabolic process
A0110154biological_processRNA decapping
A0140932molecular_function5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity
A0140933molecular_function5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity
A1901907biological_processdiadenosine pentaphosphate catabolic process
A1901909biological_processdiadenosine hexaphosphate catabolic process
A1901911biological_processadenosine 5'-(hexahydrogen pentaphosphate) catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 2361
ChainResidue
ASER28
ASER30
AGLU31
AGLU32
AGLU33
AHOH4004

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 3001
ChainResidue
ALYS133
AVAL135
AGLN136
ATYR139
AHOH4005
AHOH4010
AHOH4075
AHOH4237
AARG20
AASN86
AHIS91

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE IHP A 2360
ChainResidue
AARG10
ALYS18
AARG20
ASER39
AARG41
AARG89
AHIS91
ALYS133
AHOH4027
AHOH4031
AHOH4037
AHOH4049
AHOH4051
AHOH4053
AHOH4054
AHOH4060
AHOH4083
AHOH4089
AHOH4224

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GgmepeEepsvAAvREVcEEaG
ChainResidueDetails
AGLY51-GLY72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AGLU69

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:19585659, ECO:0007744|PDB:2FVV, ECO:0007744|PDB:2Q9P
ChainResidueDetails
AARG10
ALYS18
ASER39
AARG89
ALYS133

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19585659, ECO:0007744|PDB:2Q9P
ChainResidueDetails
AGLY50
AGLU66
AGLU70
AARG115

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

218853

PDB entries from 2024-04-24

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