Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2O28

Crystal Structure of GNPNAT1

Replaces:  2HV0
Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0004343molecular_functionglucosamine 6-phosphate N-acetyltransferase activity
A0005515molecular_functionprotein binding
A0005768cellular_componentendosome
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0010008cellular_componentendosome membrane
A0016020cellular_componentmembrane
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0042802molecular_functionidentical protein binding
B0000139cellular_componentGolgi membrane
B0004343molecular_functionglucosamine 6-phosphate N-acetyltransferase activity
B0005515molecular_functionprotein binding
B0005768cellular_componentendosome
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0010008cellular_componentendosome membrane
B0016020cellular_componentmembrane
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0042802molecular_functionidentical protein binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:18675810, ECO:0000305|PubMed:18601654, ECO:0007744|PDB:3CXQ
ChainResidueDetails
ATHR61
BTYR151
BGLU175
BARG181
ALYS108
AGLU120
ATYR151
AGLU175
AARG181
BTHR61
BLYS108
BGLU120

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:18601654, ECO:0007744|PDB:2O28
ChainResidueDetails
AGLY130
ATYR165
BGLY130
BTYR165

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon