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1RO9

CRYSTAL STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHODIESTERASE 4B2B COMPLEXED WITH 8-Br-AMP

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 529
ChainResidue
AHIS238
AHIS274
AASP275
AASP392
A8BR531

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 530
ChainResidue
AHOH658
AASP275
A8BR531
AHOH549
AHOH553

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 529
ChainResidue
BHIS238
BHIS274
BASP275
BASP392
B8BR531

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 530
ChainResidue
BASP275
B8BR531
BHOH533
BHOH545
BHOH550

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 8BR A 531
ChainResidue
ATYR233
AHIS234
AASP392
ALEU393
AASN395
ATYR403
APHE414
AGLN443
APHE446
AZN529
AZN530

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 8BR B 531
ChainResidue
BTYR233
BHIS234
BHIS238
BMET347
BASP392
BASN395
BTYR403
BILE410
BPHE414
BGLN443
BPHE446
BZN529
BZN530
BHOH588

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 Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:15003452, ECO:0007744|PDB:1ROR
ChainResidueDetails
AHIS234
BHIS234

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5
ChainResidueDetails
AHIS234
AGLN443
BHIS234
BGLN443

site_idSWS_FT_FI3
Number of Residues2
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
BHIS238

site_idSWS_FT_FI4
Number of Residues2
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
BHIS274

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15003452, ECO:0007744|PDB:1ROR
ChainResidueDetails
AASP275
BASP275

site_idSWS_FT_FI6
Number of Residues2
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
BASP392

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:15003452, ECO:0000305|PubMed:15260978, ECO:0007744|PDB:1ROR, ECO:0007744|PDB:1TB5
ChainResidueDetails
APHE446
BPHE446

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14646
ChainResidueDetails
AALA487
AALA489
BALA487
BALA489

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PDB entries from 2024-09-18

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