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5ZZ2

Crystal structure of PDE5 in complex with inhibitor LW1634

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 Residues6
Detailsbinding site for residue ZN A 901
ChainResidue
AHIS617
AHIS653
AASP654
AASP764
ASO4903
AHOH1008

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 902
ChainResidue
AHOH1008
AHOH1018
AHOH1022
AASP654
AHOH1003
AHOH1004

site_idAC3
Number of Residues8
Detailsbinding site for residue SO4 A 903
ChainResidue
AHIS613
AHIS617
AASP654
AASP764
AZN901
A9M0904
AHOH1008
AHOH1022

site_idAC4
Number of Residues11
Detailsbinding site for residue 9M0 A 904
ChainResidue
ALEU725
ALEU765
AALA767
AILE768
AGLN775
AALA783
APHE786
APHE787
AGLN817
APHE820
ASO4903

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

site_idSWS_FT_FI2
Number of Residues4
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

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12955149
ChainResidueDetails
AGLN817

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PDB entries from 2024-07-17

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