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

1JP4

Crystal Structure of an Enzyme Displaying both Inositol-Polyphosphate 1-Phosphatase and 3'-Phosphoadenosine-5'-Phosphate Phosphatase Activities

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004441molecular_functioninositol-1,4-bisphosphate 1-phosphatase activity
A0008150biological_processbiological_process
A0008441molecular_function3'(2'),5'-bisphosphate nucleotidase activity
A0016787molecular_functionhydrolase activity
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
AASP51
AMG702
AMG703
AHOH812
AHOH840
AHOH929
AHOH1216
AHOH1218
AHOH1219
AGLU74
AASP117
AVAL119
AASP120
AGLY121
ATHR122
AAMP601
AMG701

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 701
ChainResidue
AASP117
AASP120
AASP247
APO4501
AAMP601
AMG702
AHOH840

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 702
ChainResidue
AGLU74
AASP117
AVAL119
APO4501
AMG701
AHOH811

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 703
ChainResidue
AGLU74
APO4501
AHOH929
AHOH1216
AHOH1217
AHOH1218
AHOH1219

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AMP A 601
ChainResidue
AASP120
ATHR195
AHIS198
AGLY219
AGLY220
ALYS224
APHE238
AGLY242
ACYS243
AASP247
APO4501
AMG701
AHOH828
AHOH840
AHOH853
AHOH900
AHOH929

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME A 801
ChainResidue
AGLN55
ACYS59
AILE71
AGLY73
AHOH916
AHOH1117

Functional Information from PROSITE/UniProt
site_idPS00629
Number of Residues13
DetailsIMP_1 Inositol monophosphatase family signature 1. VwVDPVDGTkeY.T
ChainResidueDetails
AVAL114-THR126

site_idPS00630
Number of Residues15
DetailsIMP_2 Inositol monophosphatase family signature 2. WDtCAPeVILhavGG
ChainResidueDetails
ATRP246-GLY260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:11812139
ChainResidueDetails
AASP51
ATHR122

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:11812139, ECO:0007744|PDB:1JP4
ChainResidueDetails
AGLU74
AASP117
AVAL119
AASP120
ATHR195
AHIS198
AGLY220
ALYS224
AASP247

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.4
ChainResidueDetails
AALA2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O95861
ChainResidueDetails
ATHR122

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O95861
ChainResidueDetails
ASER240

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9Z0S1
ChainResidueDetails
ALYS244

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ima
ChainResidueDetails
AGLU74
ATHR122

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ima
ChainResidueDetails
AASP51
ATHR122
AASP247

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon