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7BTN

Crystal structure of human inorganic pyrophosphatase with metal ions

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004427molecular_functioninorganic diphosphate phosphatase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006796biological_processphosphate-containing compound metabolic process
A0016462molecular_functionpyrophosphatase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MG A 301
ChainResidue
AGLU102
AASP116
AASP118
APRO119
AILE120
AASP121
AMG302

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
AASP121
AMG301
AHOH442
AASP116
AASP118

Functional Information from PROSITE/UniProt
site_idPS00387
Number of Residues7
DetailsPPASE Inorganic pyrophosphatase signature. DNDPIDV
ChainResidueDetails
AASP116-VAL122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP116
AASP121
AASP153

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
ASER2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS57
ALYS228

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER250

227344

PDB entries from 2024-11-13

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