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1UDU

Crystal structure of Human Phosphodiesterase 5 complexed with tadalafil(Cialis)

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AHIS617
AHIS653
AASP654
AASP764

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 1002
ChainResidue
AASP654

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2001
ChainResidue
BHIS617
BHIS653
BASP654
BASP764

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 2002
ChainResidue
BASP654
BTHR723

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CIA A 1003
ChainResidue
ATYR612
ASER663
AVAL782
AALA783
APHE786
APHE787
ALEU804
AILE813
AMET816
AGLN817
APHE820

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIA B 2003
ChainResidue
BTYR612
BGLN775
BILE778
BVAL782
BALA783
BPHE786
BLEU804
BMET816
BGLN817
BPHE820

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
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O76083
ChainResidueDetails
AHIS613
BHIS613

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12955149, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1T9R, ECO:0007744|PDB:1T9S, ECO:0007744|PDB:1TBF
ChainResidueDetails
AHIS617
AHIS653
AASP654
AASP764
BHIS617
BHIS653
BASP654
BASP764

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12955149
ChainResidueDetails
AGLN817
BGLN817

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PDB entries from 2024-07-17

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