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2DCN

Crystal structure of 2-keto-3-deoxygluconate kinase from Sulfolobus tokodaii complexed with 2-keto-6-phosphogluconate (alpha-furanose form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0008673molecular_function2-dehydro-3-deoxygluconokinase activity
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0046835biological_processcarbohydrate phosphorylation
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0008673molecular_function2-dehydro-3-deoxygluconokinase activity
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0046835biological_processcarbohydrate phosphorylation
C0000166molecular_functionnucleotide binding
C0005524molecular_functionATP binding
C0008673molecular_function2-dehydro-3-deoxygluconokinase activity
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0046835biological_processcarbohydrate phosphorylation
D0000166molecular_functionnucleotide binding
D0005524molecular_functionATP binding
D0008673molecular_function2-dehydro-3-deoxygluconokinase activity
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0046835biological_processcarbohydrate phosphorylation
E0000166molecular_functionnucleotide binding
E0005524molecular_functionATP binding
E0008673molecular_function2-dehydro-3-deoxygluconokinase activity
E0016301molecular_functionkinase activity
E0016740molecular_functiontransferase activity
E0046835biological_processcarbohydrate phosphorylation
F0000166molecular_functionnucleotide binding
F0005524molecular_functionATP binding
F0008673molecular_function2-dehydro-3-deoxygluconokinase activity
F0016301molecular_functionkinase activity
F0016740molecular_functiontransferase activity
F0046835biological_processcarbohydrate phosphorylation
G0000166molecular_functionnucleotide binding
G0005524molecular_functionATP binding
G0008673molecular_function2-dehydro-3-deoxygluconokinase activity
G0016301molecular_functionkinase activity
G0016740molecular_functiontransferase activity
G0046835biological_processcarbohydrate phosphorylation
H0000166molecular_functionnucleotide binding
H0005524molecular_functionATP binding
H0008673molecular_function2-dehydro-3-deoxygluconokinase activity
H0016301molecular_functionkinase activity
H0016740molecular_functiontransferase activity
H0046835biological_processcarbohydrate phosphorylation
I0000166molecular_functionnucleotide binding
I0005524molecular_functionATP binding
I0008673molecular_function2-dehydro-3-deoxygluconokinase activity
I0016301molecular_functionkinase activity
I0016740molecular_functiontransferase activity
I0046835biological_processcarbohydrate phosphorylation
J0000166molecular_functionnucleotide binding
J0005524molecular_functionATP binding
J0008673molecular_function2-dehydro-3-deoxygluconokinase activity
J0016301molecular_functionkinase activity
J0016740molecular_functiontransferase activity
J0046835biological_processcarbohydrate phosphorylation
K0000166molecular_functionnucleotide binding
K0005524molecular_functionATP binding
K0008673molecular_function2-dehydro-3-deoxygluconokinase activity
K0016301molecular_functionkinase activity
K0016740molecular_functiontransferase activity
K0046835biological_processcarbohydrate phosphorylation
L0000166molecular_functionnucleotide binding
L0005524molecular_functionATP binding
L0008673molecular_function2-dehydro-3-deoxygluconokinase activity
L0016301molecular_functionkinase activity
L0016740molecular_functiontransferase activity
L0046835biological_processcarbohydrate phosphorylation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q97U29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues156
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of 2-keto-3-deoxygluconate kinase from Sulfolobus tokodaii complexed with 2-keto-6-phosphogluconate.","authors":["Okazaki S.","Onda H.","Suzuki A.","Kuramitsu S.","Masui R.","Yamane T."]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues60
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q97U29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
AALA254
AGLY255
AGLY253
AASP256

site_idCSA10
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
JALA254
JGLY255
JGLY253
JASP256

site_idCSA11
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
KALA254
KGLY255
KGLY253
KASP256

site_idCSA12
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
LALA254
LGLY255
LGLY253
LASP256

site_idCSA13
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
ALYS224
AGLY253

site_idCSA14
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
BLYS224
BGLY253

site_idCSA15
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
CLYS224
CGLY253

site_idCSA16
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
DLYS224
DGLY253

site_idCSA17
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
ELYS224
EGLY253

site_idCSA18
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
FLYS224
FGLY253

site_idCSA19
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
GLYS224
GGLY253

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
BALA254
BGLY255
BGLY253
BASP256

site_idCSA20
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
HLYS224
HGLY253

site_idCSA21
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
ILYS224
IGLY253

site_idCSA22
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
JLYS224
JGLY253

site_idCSA23
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
KLYS224
KGLY253

site_idCSA24
Number of Residues2
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
LLYS224
LGLY253

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
CALA254
CGLY255
CGLY253
CASP256

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
DALA254
DGLY255
DGLY253
DASP256

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
EALA254
EGLY255
EGLY253
EASP256

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
FALA254
FGLY255
FGLY253
FASP256

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
GALA254
GGLY255
GGLY253
GASP256

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
HALA254
HGLY255
HGLY253
HASP256

site_idCSA9
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
IALA254
IGLY255
IGLY253
IASP256

247536

PDB entries from 2026-01-14

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