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4MSE

Crystal structure of PDE10A2 with fragment ZT1597 (2-({[(2S)-2-methyl-2,3-dihydro-1,3-benzothiazol-5-yl]oxy}methyl)quinoline)

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 Residues8
DetailsBINDING SITE FOR RESIDUE 2ZU A 900
ChainResidue
ATYR524
ATYR693
APRO712
AMET713
AGLU721
AGLY725
APHE729
BLEU706

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 901
ChainResidue
AHIS563
AASP564
AASP674
ANI902
AHIS529

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A 902
ChainResidue
AASP564
ANI901

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI B 901
ChainResidue
BHIS529
BHIS563
BASP564
BASP674
BNI902

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI B 902
ChainResidue
BASP564
BNI901

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 Residues634
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

246704

PDB entries from 2025-12-24

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