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6ILT

Structure of Arabidopsis thaliana Ribokinase complexed with ATP and Magnesium ion

Functional Information from GO Data
ChainGOidnamespacecontents
A0004747molecular_functionribokinase activity
A0005975biological_processcarbohydrate metabolic process
A0006014biological_processD-ribose metabolic process
A0016301molecular_functionkinase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0004747molecular_functionribokinase activity
B0005975biological_processcarbohydrate metabolic process
B0006014biological_processD-ribose metabolic process
B0016301molecular_functionkinase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ATP A 401
ChainResidue
AASN255
AMG402
AMG403
AHOH501
AHOH506
AHOH512
AHOH528
AHOH530
ALYS291
ALEU292
AGLY293
AGLY296
AILE311
AALA323
AGLY324
AALA352

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 402
ChainResidue
AATP401
AHOH501
AHOH506
AHOH530

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 403
ChainResidue
ALYS107
AATP401
AHOH514
AHOH517

site_idAC4
Number of Residues6
Detailsbinding site for residue NA A 404
ChainResidue
AASP319
ATHR321
ACYS355
AVAL358
AGLY360
ASER364

site_idAC5
Number of Residues17
Detailsbinding site for residue ATP B 401
ChainResidue
BASN255
BLYS291
BLEU292
BGLY293
BGLY296
BILE312
BVAL317
BGLY324
BALA352
BMG402
BMG403
BHOH501
BHOH504
BHOH505
BHOH515
BHOH528
BHOH540

site_idAC6
Number of Residues4
Detailsbinding site for residue MG B 402
ChainResidue
BATP401
BHOH501
BHOH542
BHOH546

site_idAC7
Number of Residues3
Detailsbinding site for residue MG B 403
ChainResidue
BLYS107
BATP401
BHOH511

site_idAC8
Number of Residues6
Detailsbinding site for residue NA B 404
ChainResidue
BASP319
BTHR321
BCYS355
BVAL358
BGLY360
BSER364

Functional Information from PROSITE/UniProt
site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDtftAAFA
ChainResidueDetails
AASP319-ALA332

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03215
ChainResidueDetails
AASP325
BASP325

site_idSWS_FT_FI2
Number of Residues26
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03215
ChainResidueDetails
AASN78
ACYS355
AVAL358
AGLY360
ASER364
BASN78
BGLY106
BGLU210
BASN255
BLYS291
BASP319
AGLY106
BTHR321
BGLY324
BASP325
BCYS355
BVAL358
BGLY360
BSER364
AGLU210
AASN255
ALYS291
AASP319
ATHR321
AGLY324
AASP325

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PDB entries from 2024-04-24

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