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5WU4

Crystal structure of human Tut1 bound with MgATP, form II

Functional Information from GO Data
ChainGOidnamespacecontents
A0016779molecular_functionnucleotidyltransferase activity
B0016779molecular_functionnucleotidyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue ATP A 1001
ChainResidue
AGLY204
AHOH1101
ASER205
AASP216
AASP218
AASN392
ASER430
ATYR432
AHIS549
AMG1002

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 1002
ChainResidue
ASER205
AASP216
AASP218
AATP1001

site_idAC3
Number of Residues1
Detailsbinding site for residue CL A 1003
ChainResidue
ATRP505

site_idAC4
Number of Residues11
Detailsbinding site for residue ATP B 1001
ChainResidue
BSER205
BASP216
BASP218
BALA389
BASN392
BSER393
BTYR432
BHIS549
BVAL551
BMG1002
BHOH1101

site_idAC5
Number of Residues4
Detailsbinding site for residue MG B 1002
ChainResidue
BSER205
BASP216
BASP218
BATP1001

site_idAC6
Number of Residues1
Detailsbinding site for residue CL B 1003
ChainResidue
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
AGLU462
APRO484
AVAL502
ALEU619
BASP216
BASP218
BGLU462
BPRO484
BVAL502
BLEU619
AASP216
AASP218

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

221051

PDB entries from 2024-06-12

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