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3GBU

Crystal structure of an uncharacterized sugar kinase PH1459 from Pyrococcus horikoshii in complex with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006000biological_processfructose metabolic process
A0008865molecular_functionfructokinase activity
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0046835biological_processcarbohydrate phosphorylation
B0005524molecular_functionATP binding
B0006000biological_processfructose metabolic process
B0008865molecular_functionfructokinase activity
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0046835biological_processcarbohydrate phosphorylation
C0005524molecular_functionATP binding
C0006000biological_processfructose metabolic process
C0008865molecular_functionfructokinase activity
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0046835biological_processcarbohydrate phosphorylation
D0005524molecular_functionATP binding
D0006000biological_processfructose metabolic process
D0008865molecular_functionfructokinase activity
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0046835biological_processcarbohydrate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP A 900
ChainResidue
AARG164
AGLY246
AALA276
AHOH333
AHOH353
AHOH354
AHOH355
AHOH387
AHOH460
AHOH476
AHOH510
ALYS190
ATHR215
AGLY217
AGLY220
APHE221
AVAL237
APRO239
AALA245

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP B 900
ChainResidue
BASN162
BLYS190
BTHR215
BGLY217
BGLY220
BSER234
BTYR235
BVAL237
BALA245
BGLY246
BALA276
BHOH340
BHOH344
BHOH351
BHOH353
BHOH410

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP C 900
ChainResidue
CLYS190
CTHR215
CPHE221
CTYR235
CVAL237
CALA245
CGLY246
CASN273
CALA276
CALA277
CHOH328
CHOH338
CHOH339
CHOH361
CHOH362
CHOH366
CHOH376
CHOH381
CHOH449

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP D 900
ChainResidue
DLYS190
DTHR215
DGLY217
DPRO218
DGLY220
DPHE221
DSER234
DTYR235
DVAL237
DPRO239
DALA245
DGLY246
DALA276
DHOH329
DHOH333
DHOH340
DHOH349
DHOH403
DHOH629

Functional Information from PROSITE/UniProt
site_idPS00583
Number of Residues25
DetailsPFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGaPaNVAvgVsRLGvkssliskvG
ChainResidueDetails
AGLY33-GLY57

site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDafmAALL
ChainResidueDetails
AASP241-LEU254

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:3GBU
ChainResidueDetails
ALYS190
DLYS190
DTHR215
DGLY220
ATHR215
AGLY220
BLYS190
BTHR215
BGLY220
CLYS190
CTHR215
CGLY220

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
AALA245
AGLY246
AASP247
AGLY244

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
BALA245
BGLY246
BASP247
BGLY244

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
CALA245
CGLY246
CASP247
CGLY244

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
DALA245
DGLY246
DASP247
DGLY244

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PDB entries from 2024-10-02

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