Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1MKD

crystal structure of PDE4D catalytic domain and zardaverine complex

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
E0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
E0007165biological_processsignal transduction
E0008081molecular_functionphosphoric diester hydrolase activity
F0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
F0007165biological_processsignal transduction
F0008081molecular_functionphosphoric diester hydrolase activity
G0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
G0007165biological_processsignal transduction
G0008081molecular_functionphosphoric diester hydrolase activity
H0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
H0007165biological_processsignal transduction
H0008081molecular_functionphosphoric diester hydrolase activity
I0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
I0007165biological_processsignal transduction
I0008081molecular_functionphosphoric diester hydrolase activity
J0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
J0007165biological_processsignal transduction
J0008081molecular_functionphosphoric diester hydrolase activity
K0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
K0007165biological_processsignal transduction
K0008081molecular_functionphosphoric diester hydrolase activity
L0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
L0007165biological_processsignal transduction
L0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 2001
ChainResidue
AHIS261
AHIS297
AASP298
AASP415
AHOH1001

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 2002
ChainResidue
AASP298
AGLU327
ATHR368

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 2003
ChainResidue
BHIS297
BASP298
BASP415
BMG2004
BHIS261

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 2004
ChainResidue
BASP298
BZN2003

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 2005
ChainResidue
CHIS261
CHIS297
CASP298
CASP415

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 2006
ChainResidue
CASP298
CGLU327

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 2007
ChainResidue
DHIS261
DHIS297
DASP298
DASP415

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG D 2008
ChainResidue
DASP298

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 2009
ChainResidue
EHIS261
EHIS297
EASP298
EASP415

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG E 2010
ChainResidue
EHIS297
EASP298
EGLU327
ETHR368

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 2011
ChainResidue
FHIS261
FHIS297
FASP298
FASP415

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG F 2012
ChainResidue
FASP298
FGLU327

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 2013
ChainResidue
GHIS261
GHIS297
GASP298
GASP415

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG G 2014
ChainResidue
GASP298
GGLU327

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 2015
ChainResidue
HHIS261
HHIS297
HASP298
HASP415

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG H 2016
ChainResidue
HASP298
HGLU327

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN I 2017
ChainResidue
IHIS261
IHIS297
IASP298
IASP415

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG I 2018
ChainResidue
IASP298
IGLU327

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN J 2019
ChainResidue
JHIS261
JHIS297
JASP298
JASP415
JMG2020

site_idCC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG J 2020
ChainResidue
JASP298
JZN2019

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN K 2021
ChainResidue
KHIS261
KHIS297
KASP298
KASP415

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG K 2022
ChainResidue
KHIS297
KASP298
KTHR368

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN L 2023
ChainResidue
LHIS261
LHIS297
LASP298
LASP415

site_idCC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG L 2024
ChainResidue
LASP298
LGLU327

site_idCC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAR A 3001
ChainResidue
AMET370
AASN418
APRO419
ATYR426
ATRP429
ATHR430
AILE433
AMET454
AGLN466
APHE469

site_idCC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAR B 3002
ChainResidue
BMET370
BASN418
BPRO419
BTYR426
BTRP429
BTHR430
BILE433
BMET454
BGLN466
BPHE469

site_idCC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAR C 3003
ChainResidue
CASN418
CPRO419
CTYR426
CTRP429
CTHR430
CILE433
CMET454
CGLN466
CPHE469
CMET370

site_idDC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAR D 3004
ChainResidue
DMET370
DASN418
DPRO419
DTYR426
DTRP429
DTHR430
DILE433
DMET454
DGLN466
DPHE469

site_idDC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAR E 3005
ChainResidue
EMET370
EASN418
EPRO419
ETYR426
ETRP429
ETHR430
EILE433
EMET454
EGLN466
EPHE469

site_idDC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAR F 3006
ChainResidue
FMET370
FASN418
FPRO419
FTYR426
FTRP429
FTHR430
FILE433
FMET454
FGLN466
FPHE469

site_idDC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ZAR G 3007
ChainResidue
GMET370
GASN418
GPRO419
GTYR426
GTRP429
GTHR430
GILE433
GMET454
GGLN466
GPHE469
GHOH1007

site_idDC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAR H 3008
ChainResidue
HMET370
HASN418
HPRO419
HTYR426
HTRP429
HTHR430
HILE433
HMET454
HGLN466
HPHE469

site_idDC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ZAR I 3009
ChainResidue
IMET370
IASN418
ITYR426
ITRP429
ITHR430
IILE433
IMET454
IGLN466
IPHE469

site_idDC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAR J 3010
ChainResidue
JMET370
JASN418
JPRO419
JTYR426
JTRP429
JTHR430
JILE433
JMET454
JGLN466
JPHE469

site_idDC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ZAR K 3011
ChainResidue
KMET370
KASN418
KTYR426
KTRP429
KTHR430
KILE433
KMET454
KGLN466
KPHE469

site_idDC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAR L 3012
ChainResidue
LMET370
LASN418
LPRO419
LTYR426
LTRP429
LTHR430
LILE433
LMET454
LGLN466
LPHE469

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF
ChainResidueDetails
AHIS297-PHE308

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q07343","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14609333","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15260978","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PTW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TB7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14609333","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15260978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15576036","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17582435","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PTW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TB7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XOM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XON","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XOQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PW3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14609333","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15260978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15576036","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17582435","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PTW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TB7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XOM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XON","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XOQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XOR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PW3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14609333","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PTW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon