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3IKH

Crystal structure of Ribokinase in Complex with ATP and glycerol in the active site from Klebsiella pneumoniae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004747molecular_functionribokinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006014biological_processD-ribose metabolic process
A0016301molecular_functionkinase activity
A0019303biological_processD-ribose catabolic process
A0044281biological_processsmall molecule metabolic process
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
B0004747molecular_functionribokinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006014biological_processD-ribose metabolic process
B0016301molecular_functionkinase activity
B0019303biological_processD-ribose catabolic process
B0044281biological_processsmall molecule metabolic process
B0046835biological_processcarbohydrate phosphorylation
B0046872molecular_functionmetal ion binding
C0004747molecular_functionribokinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006014biological_processD-ribose metabolic process
C0016301molecular_functionkinase activity
C0019303biological_processD-ribose catabolic process
C0044281biological_processsmall molecule metabolic process
C0046835biological_processcarbohydrate phosphorylation
C0046872molecular_functionmetal ion binding
D0004747molecular_functionribokinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006014biological_processD-ribose metabolic process
D0016301molecular_functionkinase activity
D0019303biological_processD-ribose catabolic process
D0044281biological_processsmall molecule metabolic process
D0046835biological_processcarbohydrate phosphorylation
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP A 900
ChainResidue
AASN182
AHOH328
AHOH331
AHOH346
AHOH360
AHOH390
ATHR200
AGLY202
AGLY205
AVAL220
AGLY231
APHE234
AALA261
AHOH306

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATP B 900
ChainResidue
BLYS39
BASN182
BTHR200
BGLN201
BGLY202
BALA203
BGLY205
BVAL220
BALA230
BGLY231
BPHE234
BALA261
BHOH302
BHOH308
BHOH311
BHOH317
BHOH319
BHOH324
BHOH344
BHOH358
BHOH370
BHOH375
BHOH395

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATP C 900
ChainResidue
CASN182
CTHR200
CGLN201
CGLY202
CALA203
CGLY205
CVAL220
CGLY229
CALA230
CGLY231
CPHE234
CALA261
CHOH300
CHOH303
CHOH304
CHOH330
CHOH336
CHOH360
CHOH377
CHOH387
CHOH388
CHOH391
CHOH393

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL C 501
ChainResidue
CTHR10
CASP12
CGLY38
CASN42
CSER93
CASP232
CHOH330
CHOH367

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP D 900
ChainResidue
DLYS39
DASN182
DTHR200
DGLN201
DGLY202
DALA203
DGLY205
DVAL220
DALA230
DGLY231
DPHE234
DALA261
DHOH300
DHOH316
DHOH328
DHOH334
DHOH353
DHOH356
DHOH358
DHOH361

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 501
ChainResidue
DTHR10
DASP12
DGLY38
DASN42
DSER93
DASP232
DHOH356

Functional Information from PROSITE/UniProt
site_idPS00583
Number of Residues25
DetailsPFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGkGaNQAiiLsRCGietrliaatG
ChainResidueDetails
AGLY37-GLY61

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
AGLY231
AGLY229
AASP232
AALA230

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
BGLY231
BGLY229
BASP232
BALA230

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
CGLY231
CGLY229
CASP232
CALA230

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
DGLY231
DGLY229
DASP232
DALA230

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PDB entries from 2024-11-06

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