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3I8V

Crystal structure of human PDE4a with 4-(3-butoxy-4-methoxyphenyl)methyl-2-imidazolidone

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 Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
AHOH114
AHIS376
AHIS412
AASP413
AASP530
AHOH634

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 623
ChainResidue
AHOH151
AHOH174
AASP413
AHOH6
AHOH64
AHOH114

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0MO A 1
ChainResidue
AHOH105
ATYR371
ATHR483
AMET485
AASN533
ATHR545
AILE548
APHE552
AMET569
AGLN581
APHE584
AHOH634

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 3
ChainResidue
AHIS366
AASP415
APRO417
AHOH685
AHOH686
BHIS366

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CO A 624
ChainResidue
AASP368
AHOH679
BHOH682

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 1
ChainResidue
BHOH74
BHIS376
BHIS412
BASP413
BASP530
BHOH636

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 623
ChainResidue
BHOH38
BHOH60
BHOH69
BHOH74
BHOH162
BASP413

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 0MO B 2
ChainResidue
BHOH60
BHOH155
BMET485
BASP530
BTHR545
BILE548
BMET549
BPHE552
BGLN581
BPHE584
BHOH636

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 624
ChainResidue
AGLU500
BASP586
BHIS590
BARG615

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 625
ChainResidue
BHOH262
BTHR390
BASP603
BILE607

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF
ChainResidueDetails
AHIS412-PHE423

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q07343
ChainResidueDetails
AHIS372
BHIS372

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q07343
ChainResidueDetails
AHIS372
AASP413
AGLN581
APHE584
BHIS372
BASP413
BGLN581
BPHE584

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17727341, ECO:0000269|Ref.20, ECO:0007744|PDB:2QYK, ECO:0007744|PDB:3I8V
ChainResidueDetails
AHIS376
AHIS412
AASP530
BHIS376
BHIS412
BASP530

site_idSWS_FT_FI4
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:20196770
ChainResidueDetails
ALYS297
BLYS297

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PDB entries from 2024-11-13

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