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3QPN

Structure of PDE10-inhibitor complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
A0007165biological_processsignal transduction
A0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 997
ChainResidue
APHE472
AGLU473
AASN474
AARG510
AARG558

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AASP664
AHOH3
AHIS519
AHIS553
AASP554

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 2
ChainResidue
AHOH3
AHOH4
AHOH5
AASP554
AHOH785
AHOH786

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PFK A 999
ChainResidue
AHIS647
ALEU665
AVAL668
ATYR683
APHE686
APRO702
AMET703
ALYS708
AGLY715
AGLN716
APHE719

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHrGfsNsY
ChainResidueDetails
AHIS553-TYR564

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O76083","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y233","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17228859","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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