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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 Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:28589955, ECO:0007744|PDB:5WU4
ChainResidueDetails
ASER205
BSER205

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:28589955, ECO:0007744|PDB:5WU2, ECO:0007744|PDB:5WU3
ChainResidueDetails
AASP216
BPRO484
BVAL502
BLEU619
AASP218
AGLU462
APRO484
AVAL502
ALEU619
BASP216
BASP218
BGLU462

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3MHT4
ChainResidueDetails

222415

PDB entries from 2024-07-10

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