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3KT7

Crystal structure of Tpa1 from Saccharomyces cerevisiae, a component of the messenger ribonucleoprotein complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000288biological_processnuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
A0005506molecular_functioniron ion binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006415biological_processtranslational termination
A0006449biological_processregulation of translational termination
A0006450biological_processregulation of translational fidelity
A0008143molecular_functionpoly(A) binding
A0008198molecular_functionferrous iron binding
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0018188biological_processpeptidyl-proline di-hydroxylation
A0031418molecular_functionL-ascorbic acid binding
A0031543molecular_functionpeptidyl-proline dioxygenase activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 701
ChainResidue
AHIS159
AASP161
AHIS227
AAKG702
AHOH1495

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE AKG A 702
ChainResidue
ATYR173
AHIS227
ALVN229
AARG238
AGLN242
AFE701
AHOH859
AHOH1151
AHOH1167
AHOH1414
AHOH1495
ALEU156
AHIS159
AASP161
AILE171

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 A 703
ChainResidue
AALA544
AGLY545
AGLY545
ATRP546
ATRP546
AGLU547
AGLU547
ASER548
ASER548
AHOH985
AHOH985

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 704
ChainResidue
ALYS152
AVAL234
AASP235
AHOH1444

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 705
ChainResidue
AARG179
ALYS180
ALYS182
AHOH1204

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 706
ChainResidue
ALYS180
ALYS182
ASER183
AHOH922
AHOH979
AHOH1180
AHOH1276

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 707
ChainResidue
AARG423
AASN424
AHOH1051
AHOH1337

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:20040577, ECO:0000269|PubMed:25728928
ChainResidueDetails
AHIS159
AASP161
AHIS227

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:20040577
ChainResidueDetails
ATYR173

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:20040577
ChainResidueDetails
AARG238

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER607

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PDB entries from 2024-03-27

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