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3FB3

Crystal Structure of Trypanosoma Brucei Acetyltransferase, Tb11.01.2886

Functional Information from GO Data
ChainGOidnamespacecontents
A0004343molecular_functionglucosamine 6-phosphate N-acetyltransferase activity
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0008080molecular_functionN-acetyltransferase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0020015cellular_componentglycosome
A0030311biological_processpoly-N-acetyllactosamine biosynthetic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
B0004343molecular_functionglucosamine 6-phosphate N-acetyltransferase activity
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0008080molecular_functionN-acetyltransferase activity
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0020015cellular_componentglycosome
B0030311biological_processpoly-N-acetyllactosamine biosynthetic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P43577","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ygh
ChainResidueDetails
AHIS80

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ygh
ChainResidueDetails
BHIS80

246031

PDB entries from 2025-12-10

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