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4DB3

1.95 Angstrom Resolution Crystal Structure of N-acetyl-D-glucosamine kinase from Vibrio vulnificus.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006044biological_processN-acetylglucosamine metabolic process
A0008270molecular_functionzinc ion binding
A0009254biological_processpeptidoglycan turnover
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0045127molecular_functionN-acetylglucosamine kinase activity
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS157
ACYS177
ACYS179
ACYS184

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 402
ChainResidue
AARG294

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 403
ChainResidue
AGLY254

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
AARG98
ASER99
AHOH561

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
APRO123
AVAL144
APHE145
ASER146
AGLY147
AHIS247
AHOH563
AHOH582
AHOH634

Functional Information from PROSITE/UniProt
site_idPS01125
Number of Residues28
DetailsROK ROK family signature. LgtGFGgGLiyeGkvfsGrnnvaGElGH
ChainResidueDetails
ALEU130-HIS157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01271
ChainResidueDetails
AGLY4
AGLY133
AHIS157
ACYS177
ACYS179
ACYS184

224201

PDB entries from 2024-08-28

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