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2Q0G

Terminal uridylyl transferase 4 from Trypanosoma brucei with bound UPU

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
AASP136
AUPU501
AHOH552

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BASP66
BASP68
BASP136
BUPU502

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
AHIS246
AHIS250
AHOH523
AHOH610

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 404
ChainResidue
BHIS246
BHIS250
BHOH504
BHOH552

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE UPU A 501
ChainResidue
APHE52
AGLY53
AASP68
AARG121
AARG126
AASP136
AGLY144
AASN147
ASER148
ATYR189
AMG401
AHOH502
AHOH505
AHOH512
AHOH535
AHOH552
AHOH592
AHOH600

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE UPU B 502
ChainResidue
BPHE52
BGLY53
BASP66
BASP68
BARG121
BVAL122
BGLY144
BASN147
BSER148
BTYR189
BMG402
BHOH503
BHOH517
BHOH532
BHOH535

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

223790

PDB entries from 2024-08-14

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