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2A2C

x-ray structure of human N-acetyl galactosamine kinase complexed with Mg-ADP and N-acetyl galactosamine 1-phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004335molecular_functiongalactokinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006012biological_processgalactose metabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0033858molecular_functionN-acetylgalactosamine kinase activity
A0046835biological_processcarbohydrate phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00106
Number of Residues12
DetailsGALACTOKINASE Galactokinase signature. GRvNIIGEHiDY
ChainResidueDetails
AGLY42-TYR53

site_idPS00627
Number of Residues12
DetailsGHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. IPpSsGLSSSSA
ChainResidueDetails
AILE138-ALA149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9HHB6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"Q9HHB6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fwk
ChainResidueDetails
ALYS234

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fwk
ChainResidueDetails
AALA332

239492

PDB entries from 2025-07-30

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