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2Q0D

Terminal uridylyl transferase 4 from Trypanosoma brucei with bound ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0016779molecular_functionnucleotidyltransferase activity
A0020023cellular_componentkinetoplast
A0046872molecular_functionmetal ion binding
A0050265molecular_functionRNA uridylyltransferase activity
A0071076biological_processRNA 3' uridylation
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0016779molecular_functionnucleotidyltransferase activity
B0020023cellular_componentkinetoplast
B0046872molecular_functionmetal ion binding
B0050265molecular_functionRNA uridylyltransferase activity
B0071076biological_processRNA 3' uridylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP66
AASP68
AATP501
AHOH507
AHOH664

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHOH636
AHOH665
AHOH670
AHOH671
AATP501
AHOH507
AHOH515
AHOH615

site_idAC3
Number of Residues30
DetailsBINDING SITE FOR RESIDUE ATP A 501
ChainResidue
APHE52
AGLY53
ASER54
ASER65
AASP66
AASP68
AARG121
AGLY144
AASN147
ASER148
ALYS169
ALYS173
ATHR187
ASER188
ATYR189
ALEU303
AVAL305
AARG307
AMG401
AMG402
AHOH505
AHOH507
AHOH515
AHOH548
AHOH551
AHOH556
AHOH579
AHOH636
AHOH664
AHOH672

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:17189640, ECO:0000269|PubMed:17785418, ECO:0000269|PubMed:27744351, ECO:0007744|PDB:2IKF, ECO:0007744|PDB:2Q0F, ECO:0007744|PDB:5KAL
ChainResidueDetails
ASER54
BLYS169
BLYS173
BSER188
ASER65
AGLY144
ALYS169
ALYS173
ASER188
BSER54
BSER65
BGLY144

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17189640, ECO:0000269|PubMed:17785418, ECO:0000269|PubMed:27744351, ECO:0007744|PDB:2IKF, ECO:0007744|PDB:2NOM, ECO:0007744|PDB:2Q0C, ECO:0007744|PDB:2Q0D, ECO:0007744|PDB:2Q0E, ECO:0007744|PDB:2Q0F, ECO:0007744|PDB:2Q0G, ECO:0007744|PDB:5KAL
ChainResidueDetails
AASP66
AASP68
BASP66
BASP68

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17785418, ECO:0000269|PubMed:27744351, ECO:0007744|PDB:2Q0F, ECO:0007744|PDB:2Q0G, ECO:0007744|PDB:5KAL
ChainResidueDetails
AARG121
BARG121

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:17189640
ChainResidueDetails
AASP136
BASP136

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fa0
ChainResidueDetails
ALYS169

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fa0
ChainResidueDetails
BLYS169

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PDB entries from 2024-07-17

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