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2OVV

Crystal structure of the catalytic domain of rat phosphodiesterase 10A

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 Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 997
ChainResidue
AHOH128
AHOH139
AHOH210
AHOH220
APHE472
AGLU473
AASN474
AARG510
AARG558

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 9001
ChainResidue
AHOH3
AHIS519
AHIS553
AASP554
AASP664

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 9002
ChainResidue
AHOH1
AHOH2
AHOH3
AHOH4
AHOH5
AASP554

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PFH A 999
ChainResidue
AHOH54
AHOH117
APHE629
AHIS647
ALEU665
AVAL668
APHE686
AGLN716
AGLY718
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 2024-07-17

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