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2CH5

Crystal structure of human N-acetylglucosamine kinase in complex with N-acetylglucosamine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006044biological_processN-acetylglucosamine metabolic process
A0006046biological_processN-acetylglucosamine catabolic process
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0006051biological_processN-acetylmannosamine metabolic process
A0009384molecular_functionN-acylmannosamine kinase activity
A0019262biological_processN-acetylneuraminate catabolic process
A0032495biological_processresponse to muramyl dipeptide
A0042742biological_processdefense response to bacterium
A0045127molecular_functionN-acetylglucosamine kinase activity
A0070062cellular_componentextracellular exosome
A0070434biological_processpositive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway
A0160047molecular_functionmuramyl dipeptide kinase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006044biological_processN-acetylglucosamine metabolic process
B0006046biological_processN-acetylglucosamine catabolic process
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0006051biological_processN-acetylmannosamine metabolic process
B0009384molecular_functionN-acylmannosamine kinase activity
B0019262biological_processN-acetylneuraminate catabolic process
B0032495biological_processresponse to muramyl dipeptide
B0042742biological_processdefense response to bacterium
B0045127molecular_functionN-acetylglucosamine kinase activity
B0070062cellular_componentextracellular exosome
B0070434biological_processpositive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway
B0160047molecular_functionmuramyl dipeptide kinase activity
C0005515molecular_functionprotein binding
C0005829cellular_componentcytosol
C0006044biological_processN-acetylglucosamine metabolic process
C0006046biological_processN-acetylglucosamine catabolic process
C0006048biological_processUDP-N-acetylglucosamine biosynthetic process
C0006051biological_processN-acetylmannosamine metabolic process
C0009384molecular_functionN-acylmannosamine kinase activity
C0019262biological_processN-acetylneuraminate catabolic process
C0032495biological_processresponse to muramyl dipeptide
C0042742biological_processdefense response to bacterium
C0045127molecular_functionN-acetylglucosamine kinase activity
C0070062cellular_componentextracellular exosome
C0070434biological_processpositive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway
C0160047molecular_functionmuramyl dipeptide kinase activity
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0006044biological_processN-acetylglucosamine metabolic process
D0006046biological_processN-acetylglucosamine catabolic process
D0006048biological_processUDP-N-acetylglucosamine biosynthetic process
D0006051biological_processN-acetylmannosamine metabolic process
D0009384molecular_functionN-acylmannosamine kinase activity
D0019262biological_processN-acetylneuraminate catabolic process
D0032495biological_processresponse to muramyl dipeptide
D0042742biological_processdefense response to bacterium
D0045127molecular_functionN-acetylglucosamine kinase activity
D0070062cellular_componentextracellular exosome
D0070434biological_processpositive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway
D0160047molecular_functionmuramyl dipeptide kinase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17010375","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2CH6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17010375","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CH5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"12112843","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

253389

PDB entries from 2026-05-13

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