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1KNQ

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 CL A 200
ChainResidue
AGLY18
ASER19
AGLY20
ALYS21
AHOH434

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 201
ChainResidue
BHOH287
BGLY18
BSER19
BGLY20
BLYS21

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 417
ChainResidue
AHIS127
ALYS130
AHOH450
AHOH484

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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