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1XOR

Catalytic Domain Of Human Phosphodiesterase 4D In Complex With Zardaverine

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 1001
ChainResidue
AHIS164
AHIS200
AASP201
AASP318
AZAR701
AHOH1007

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1002
ChainResidue
AHOH1005
AHOH1006
AHOH1007
AASP201
AHOH1003
AHOH1004

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 1001
ChainResidue
BHIS164
BHIS200
BASP201
BASP318
BZAR704
BHOH2007

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1002
ChainResidue
BASP201
BHOH2003
BHOH2004
BHOH2005
BHOH2006
BHOH2007

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ZAR A 701
ChainResidue
ATYR159
AHIS160
AHIS164
AASP201
AMET273
AASP318
AASN321
APRO322
ATYR329
ATRP332
ATHR333
AILE336
APHE340
AMET357
ASER368
AGLN369
APHE372
AZN1001
AHOH1006
AHOH1007
AHOH1283

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ZAR B 704
ChainResidue
BTYR159
BHIS160
BHIS164
BASP201
BASP318
BASN321
BPRO322
BTYR329
BTRP332
BTHR333
BILE336
BPHE340
BMET357
BSER368
BGLN369
BPHE372
BZN1001
BHOH2006
BHOH2007
BHOH2131
BHOH2271
BHOH2277

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF
ChainResidueDetails
AHIS200-PHE211

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q07343
ChainResidueDetails
AHIS160
BHIS160

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7
ChainResidueDetails
AHIS160
AASN321
AGLN369
BHIS160
BASN321
BGLN369

site_idSWS_FT_FI3
Number of Residues2
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
AHIS164
BHIS164

site_idSWS_FT_FI4
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:1XOR, ECO:0007744|PDB:2PW3
ChainResidueDetails
AHIS200
AASP318
BHIS200
BASP318

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW
ChainResidueDetails
AASP201
APHE372
BASP201
BPHE372

222036

PDB entries from 2024-07-03

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