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6IJI

Crystal structure of PDE10 in complex with inhibitor 2b

Functional Information from GO Data
ChainGOidnamespacecontents
A0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
A0007165biological_processsignal transduction
A0008081molecular_functionphosphoric diester hydrolase activity
B0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
B0007165biological_processsignal transduction
B0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 801
ChainResidue
AHIS529
AHIS563
AASP564
AASP674
AHOH912

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 802
ChainResidue
AHOH912
AASP564
AGLU592
AHOH901
AHOH908

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 801
ChainResidue
BHIS529
BHIS563
BASP564
BASP674

site_idAC4
Number of Residues5
Detailsbinding site for residue MG B 802
ChainResidue
BASP564
BGLU592
BHOH902
BHOH904
BHOH918

site_idAC5
Number of Residues9
Detailsbinding site for residue AEL B 803
ChainResidue
BTYR524
BLEU675
BILE692
BTYR693
BMET713
BGLY725
BGLN726
BPHE729
BHOH903

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHrGfsNsY
ChainResidueDetails
AHIS563-TYR574

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues317
DetailsDomain: {"description":"PDEase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01192","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O76083","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17389385","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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