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3QPP

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 Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AMG2
AHOH3
AHIS519
AHIS553
AASP554
AASP664

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 2
ChainResidue
AASP554
AHOH785
AHOH786
AZN1
AHOH3
AHOH4

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 997
ChainResidue
AHOH220
AGLU473
AASN474
AARG510
AARG558

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 900
ChainResidue
AHOH172
APRO513
AARG558
AGLY559
APHE560
AGLU685
AALA688

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS A 901
ChainResidue
AHOH96
AHOH254
AASP461
ALEU464
AHIS466
ALEU696

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PFW A 999
ChainResidue
AHOH171
AHIS647
AVAL668
ATYR683
APRO702
AMET703
ALYS708
AVAL712
AGLY715
AGLN716
APHE719
AVAL723

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
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O76083
ChainResidueDetails
AHIS515

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9Y233
ChainResidueDetails
AHIS515
AGLN716

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17228859
ChainResidueDetails
AHIS519
AHIS553
AASP554
AASP664

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PDB entries from 2024-07-10

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