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3DYS

human phosphodiestrase-5'GMP complex (EP), produced by soaking with 20mM cGMP+20 mM MnCl2+20 mM MgCl2 for 2 hours, and flash-cooled to liquid nitrogen temperature when substrate was still abudant.

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 MN A 901
ChainResidue
AHIS256
AHIS292
AASP293
AASP402
A5GP900

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 902
ChainResidue
AHOH1133
AASP293
A5GP900
AHOH1131
AHOH1132

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 65
ChainResidue
AASP244
ATYR246
AHOH990
AHOH1046
AHOH1110

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 901
ChainResidue
BFMT1
BHIS256
BHIS292
BASP293
BASP402
BHOH1185

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 902
ChainResidue
BASP293
BHOH1185
BHOH1186
BHOH1187
BHOH1188
BHOH1189

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 89
ChainResidue
BASP244
BTYR246
BHOH1037
BHOH1129
BHOH1147
BHOH1184

site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 5GP A 900
ChainResidue
AHIS252
AHIS256
AHIS292
AASP293
AASP402
AILE403
ALEU420
ATYR424
AALA452
AGLN453
APHE456
AMN901
AMG902
AHOH914
AHOH915
AHOH917
AHOH950
AHOH961
AHOH1038
AHOH1131

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IBM B 900
ChainResidue
AALA499
AMET500
BLEU420
BTYR424
BALA452
BGLN453
BPHE456
BHOH993
BHOH1029
BHOH1045

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT B 1
ChainResidue
BPHE251
BHIS252
BHIS256
BASP293
BASP402
BMN901
BHOH1058
BHOH1185
BHOH1186

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHpGynNtY
ChainResidueDetails
AHIS292-TYR303

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"18757755","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18757755","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18757755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19919087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20121115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21483814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22985069","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23025719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HD1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YY2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DYN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JSI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JSW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K3E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K3H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N3Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E90","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G2L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GH6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8QZV1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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