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1KO5

Crystal structure of gluconate kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0042803molecular_functionprotein homodimerization activity
A0046177biological_processD-gluconate catabolic process
A0046316molecular_functiongluconokinase activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0042803molecular_functionprotein homodimerization activity
B0046177biological_processD-gluconate catabolic process
B0046316molecular_functiongluconokinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1001
ChainResidue
ASER22
AATP302
AHOH1011
AHOH1018
AHOH1033

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1002
ChainResidue
BHOH1036
BSER22
BATP303
BHOH1025
BHOH1035

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP A 302
ChainResidue
AVAL16
ASER17
AGLY18
ASER19
AGLY20
ALYS21
ASER22
AALA23
AARG120
AARG124
AGLN158
APRO159
ALEU160
AMG1001
AHOH1011
AHOH1018
AHOH1033

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP B 303
ChainResidue
BVAL16
BSER17
BGLY18
BSER19
BGLY20
BLYS21
BSER22
BALA23
BARG120
BARG124
BILE156
BGLN158
BLEU160
BVAL163
BMG1002
BHOH1025
BHOH1035
BHOH1036

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AVAL16
BVAL16

218853

PDB entries from 2024-04-24

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