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2NOM

Terminal uridylyl transferase 4 from Trypanosoma brucei with bound dUTP

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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP66
AASP68
AMG402
ADUT501
AHOH556
AHOH590

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AMG401
AHOH588
AHOH589
AHOH590
AASP66
AASP68
AASP136

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE DUT A 501
ChainResidue
APHE52
AGLY53
ASER54
AVAL57
ASER65
AASP66
AASP68
AASN147
ASER148
ALEU151
ALYS169
ALYS173
ATHR187
ASER188
ATYR189
AMG401
AHOH525
AHOH540
AHOH556
AHOH558
AHOH573
AHOH574
AHOH576
AHOH587
AHOH590

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE DUT B 502
ChainResidue
BGLY53
BSER54
BASP66
BASP68
BASN147
BSER148
BLYS169
BLYS173
BTHR187
BSER188
BTYR189
BHOH533

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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