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3FRG

Catalytic Domain of Human Phosphodiesterase 4B2B in Complex with a Quinoline Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004114molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity
A0007165biological_processsignal transduction
A0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SK4 A 1
ChainResidue
ATYR233
AHOH523
AHOH789
ATHR345
AMET347
AASP392
AASN395
AMET431
AGLN443
APHE446
AHOH513

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 504
ChainResidue
AHIS238
AHIS274
AASP275
AASP392
AHOH581
AHOH668

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 505
ChainResidue
AASP275
AHOH579
AHOH580
AHOH581
AHOH582
AHOH585

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ARS A 506
ChainResidue
APHE156
ACYS194

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ARS A 2
ChainResidue
AGLU317
ACYS320

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ARS A 3
ChainResidue
ASER429
ACYS432

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 507
ChainResidue
AASP277
AGLU292
AHOH518
AHOH544
AHOH622
AHOH702
AHOH826

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 508
ChainResidue
ATYR449
AHOH827
AHOH828

Functional Information from PROSITE/UniProt
site_idPS00126
Number of Residues12
DetailsPDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF
ChainResidueDetails
AHIS274-PHE285

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:15003452, ECO:0007744|PDB:1ROR
ChainResidueDetails
AHIS234

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5
ChainResidueDetails
AHIS234
AGLN443

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:2QYL, ECO:0007744|PDB:3D3P
ChainResidueDetails
AHIS238

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1F0J, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:2QYL, ECO:0007744|PDB:3D3P
ChainResidueDetails
AHIS274

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0007744|PDB:1ROR
ChainResidueDetails
AASP275

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10846163, ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:15685167, ECO:0000269|PubMed:18539455, ECO:0007744|PDB:1F0J, ECO:0007744|PDB:1RO6, ECO:0007744|PDB:1RO9, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5, ECO:0007744|PDB:1XLX, ECO:0007744|PDB:1XLZ, ECO:0007744|PDB:1XM4, ECO:0007744|PDB:1XM6, ECO:0007744|PDB:1XMU, ECO:0007744|PDB:1XMY, ECO:0007744|PDB:1XN0, ECO:0007744|PDB:1XOS, ECO:0007744|PDB:1XOT, ECO:0007744|PDB:1Y2H, ECO:0007744|PDB:1Y2J, ECO:0007744|PDB:3D3P
ChainResidueDetails
AASP392

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:15003452, ECO:0000305|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5
ChainResidueDetails
APHE446

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14646
ChainResidueDetails
AALA487
AALA489

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PDB entries from 2024-07-10

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