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4MD6

Crystal structure of PDE5 in complex with inhibitor 5R

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
AHIS613
AHIS617
AASP654
AASP764
A24E902
AZN903
AHOH1002

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 24E A 902
ChainResidue
AILE768
AGLN775
AVAL782
AALA783
APHE787
AILE813
AMET816
AGLN817
APHE820
ASO4901
ALEU725
AALA767

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 903
ChainResidue
AHIS617
AHIS653
AASP654
AASP764
ASO4901
AMG904
AHOH1001

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 904
ChainResidue
AASP654
AZN903
AHOH1001
AHOH1002
AHOH1003
AHOH1004
AHOH1005

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 Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O76083","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
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 Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12955149","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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