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6VBI

crystal structure of PDE5 in complex with a non-competitive inhibitor

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 Residues16
Detailsbinding site for residue FZA A 901
ChainResidue
AASP563
AASP764
ASER766
AALA767
AILE778
AHOH1067
BMET691
BSER695
APHE564
AALA611
AASN614
AARG616
AHIS617
AASN620
ATHR621
ACYS763

site_idAC2
Number of Residues13
Detailsbinding site for residue FZA B 901
ChainResidue
BASP563
BALA611
BASN614
BARG616
BHIS617
BASN620
BTHR621
BCYS763
BASP764
BSER766
BALA767
BILE778
BHOH1044

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHrGvnNsY
ChainResidueDetails
AHIS653-TYR664

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O76083","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12955149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15260978","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T9R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TBF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12955149","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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