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3G4G

Crystal structure of human phosphodiesterase 4d with regulatory domain and d155871

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
C0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
C0007165biological_processsignal transduction
C0008081molecular_functionphosphoric diester hydrolase activity
D0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
D0007165biological_processsignal transduction
D0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 801
ChainResidue
AHOH50
AHIS330
AHIS366
AASP367
AASP484

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 802
ChainResidue
AHOH80
AASP367
AHOH586

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 4
ChainResidue
AHIS271

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE D71 A 901
ChainResidue
AHOH54
AHOH154
APHE196
AILE197
APHE201
ATYR325
AHIS326
ALEU485
AASN487
ATHR499
AILE502
AMET503
APHE506
ASER534
AGLN535
APHE538

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 803
ChainResidue
BHOH59
BHIS330
BHIS366
BASP367
BASP484

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 804
ChainResidue
BHOH96
BHOH118
BASP367
BHOH586

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE D71 B 902
ChainResidue
BHOH82
BVAL193
BPHE196
BILE197
BTYR325
BHIS326
BLEU485
BASN487
BTHR499
BILE502
BPHE506
BSER534
BGLN535
BPHE538

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN C 805
ChainResidue
CHOH34
CHIS330
CHIS366
CASP367
CASP484
CHOH587

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 806
ChainResidue
CHOH72
CHOH88
CASP367
CHOH587

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA C 2
ChainResidue
CHIS271
CARG274

site_idBC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE D71 C 903
ChainResidue
CHOH31
CPHE196
CILE197
CTYR325
CHIS326
CLEU485
CASN487
CTHR499
CILE502
CPHE506
CMET523
CSER534
CGLN535
CPHE538
CHOH586

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 807
ChainResidue
DHOH21
DHIS330
DHIS366
DASP367
DASP484

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 808
ChainResidue
DHOH6
DHOH67
DHOH84
DHOH140
DASP367

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA D 3
ChainResidue
DHIS271

site_idBC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE D71 D 904
ChainResidue
DHOH33
DVAL193
DPHE196
DILE197
DTYR325
DHIS326
DLEU485
DASN487
DTHR499
DILE502
DSER534
DGLN535
DPHE538

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF
ChainResidueDetails
AHIS366-PHE377

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q07343
ChainResidueDetails
AHIS326
BHIS326
CHIS326
DHIS326

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
ChainResidueDetails
AHIS326
DHIS326
DASN487
DGLN535
AASN487
AGLN535
BHIS326
BASN487
BGLN535
CHIS326
CASN487
CGLN535

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3
ChainResidueDetails
AHIS330
BHIS330
CHIS330
DHIS330

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3
ChainResidueDetails
AHIS366
AASP484
BHIS366
BASP484
CHIS366
CASP484
DHIS366
DASP484

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW
ChainResidueDetails
AASP367
APHE538
BASP367
BPHE538
CASP367
CPHE538
DASP367
DPHE538

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER163
ASER165
BSER163
BSER165
CSER163
CSER165
DSER163
DSER165

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER239
BSER239
CSER239
DSER239

site_idSWS_FT_FI8
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
ChainResidueDetails
ALYS251
BLYS251
CLYS251
DLYS251

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PDB entries from 2024-07-17

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