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1KO8

Crystal structure of gluconate kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005975biological_processcarbohydrate metabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0042803molecular_functionprotein homodimerization activity
A0046177biological_processobsolete D-gluconate catabolic process
A0046316molecular_functiongluconokinase activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005975biological_processcarbohydrate metabolic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0042803molecular_functionprotein homodimerization activity
B0046177biological_processobsolete D-gluconate catabolic process
B0046316molecular_functiongluconokinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 6PG A 502
ChainResidue
ASER17
AHOH516
AHOH517
AGLY18
AASP40
ALEU121
AHIS127
AMG201
AHOH513
AHOH514
AHOH515

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 6PG B 503
ChainResidue
BSER17
BGLY18
BLYS21
BHOH510
BHOH511
BHOH512
BHOH513

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 201
ChainResidue
ASER22
A6PG502
AHOH512
AHOH513
AHOH515
AHOH516

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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