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

7P7W

N-acetylglucosamine kinase from Plesiomonas shigelloides compexed with alpha-N-acetylglucosamine and ADP

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0000794cellular_componentcondensed nuclear chromosome
AAA0005515molecular_functionprotein binding
AAA0005524molecular_functionATP binding
AAA0005634cellular_componentnucleus
AAA0005940cellular_componentseptin ring
AAA0006044biological_processN-acetylglucosamine metabolic process
AAA0008270molecular_functionzinc ion binding
AAA0009254biological_processpeptidoglycan turnover
AAA0016301molecular_functionkinase activity
AAA0016925biological_processprotein sumoylation
AAA0031386molecular_functionprotein tag activity
AAA0042802molecular_functionidentical protein binding
AAA0044389molecular_functionubiquitin-like protein ligase binding
AAA0045127molecular_functionN-acetylglucosamine kinase activity
AAA0046835biological_processcarbohydrate phosphorylation
AAA0046872molecular_functionmetal ion binding
BBB0000794cellular_componentcondensed nuclear chromosome
BBB0005515molecular_functionprotein binding
BBB0005524molecular_functionATP binding
BBB0005634cellular_componentnucleus
BBB0005940cellular_componentseptin ring
BBB0006044biological_processN-acetylglucosamine metabolic process
BBB0008270molecular_functionzinc ion binding
BBB0009254biological_processpeptidoglycan turnover
BBB0016301molecular_functionkinase activity
BBB0016925biological_processprotein sumoylation
BBB0031386molecular_functionprotein tag activity
BBB0042802molecular_functionidentical protein binding
BBB0044389molecular_functionubiquitin-like protein ligase binding
BBB0045127molecular_functionN-acetylglucosamine kinase activity
BBB0046835biological_processcarbohydrate phosphorylation
BBB0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS01125
Number of Residues28
DetailsROK ROK family signature. LgtGVGgGLifnGkvhsGraniaGEiGH
ChainResidueDetails
AAALEU130-HIS157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950
ChainResidueDetails
AAASER-105
BBBSER-105

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358
ChainResidueDetails
AAASER-103
BBBSER-103

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon