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2WEY

Human PDE-papaverine complex obtained by ligand soaking of cross- linked protein crystals

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 EV1 B 1771
ChainResidue
BLEU635
BTYR693
BPHE696
BGLN726
BPHE729

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EV1 A 1771
ChainResidue
APHE696
AGLY725
AGLN726
APHE729
BLEU706
ATYR524
AHIS525
AILE692
AGLU695

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1772
ChainResidue
AHIS529
AHIS563
AASP564
AASP674
AHOH2013
AHOH2014

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 1773
ChainResidue
AASP564
AGLU592
AHOH2003
AHOH2005
AHOH2006
AHOH2008
AHOH2014

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 1772
ChainResidue
BHIS529
BHIS563
BASP564
BASP674
BHOH2005
BHOH2009

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 1773
ChainResidue
BASP564
BGLU592
BHOH2004
BHOH2006
BHOH2007
BHOH2008
BHOH2009

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHrGfsNsY
ChainResidueDetails
AHIS563-TYR574

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O76083
ChainResidueDetails
ATHR773
BTHR773

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18477562, ECO:0007744|PDB:2ZMF
ChainResidueDetails
AASN544
ATHR588
AVAL622
AASN641
BASN544
BTHR588
BVAL622
BASN641

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:17389385
ChainResidueDetails
ATHR773
BASP564
BASP674
BGLN726
ASER777
AHIS563
AASP564
AASP674
AGLN726
BTHR773
BSER777
BHIS563

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PDB entries from 2024-07-24

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