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5WU2

Crystal structure of human Tut1 bound with BaUTP, form I

Functional Information from GO Data
ChainGOidnamespacecontents
A0016779molecular_functionnucleotidyltransferase activity
B0016779molecular_functionnucleotidyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue UTP A 1001
ChainResidue
AGLY204
ATYR432
AHIS549
ABA1002
ASER205
AASN208
AALA389
AASN392
ASER393
AARG414
ASER430
AASN431

site_idAC2
Number of Residues3
Detailsbinding site for residue BA A 1002
ChainResidue
AASP216
AASP218
AUTP1001

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 1003
ChainResidue
AARG445
ATRP505

site_idAC4
Number of Residues13
Detailsbinding site for residue UTP B 1001
ChainResidue
BGLY204
BSER205
BASN208
BCYS215
BALA389
BASN392
BSER393
BARG414
BSER430
BASN431
BTYR432
BHIS549
BBA1002

site_idAC5
Number of Residues3
Detailsbinding site for residue BA B 1002
ChainResidue
BASP216
BASP218
BUTP1001

site_idAC6
Number of Residues2
Detailsbinding site for residue CL B 1003
ChainResidue
BARG445
BTRP505

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues116
DetailsDomain: {"description":"PAP-associated","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28589955","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WU4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28589955","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WU2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WU3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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