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6XK2

Crystal structure of Ribokinase from Cryptococcus neoformans var. grubii serotype A in complex with ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004747molecular_functionribokinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006014biological_processD-ribose metabolic process
A0016301molecular_functionkinase activity
A0019303biological_processD-ribose catabolic process
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
B0004747molecular_functionribokinase activity
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006014biological_processD-ribose metabolic process
B0016301molecular_functionkinase activity
B0019303biological_processD-ribose catabolic process
B0046835biological_processcarbohydrate phosphorylation
B0046872molecular_functionmetal ion binding
C0004747molecular_functionribokinase activity
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006014biological_processD-ribose metabolic process
C0016301molecular_functionkinase activity
C0019303biological_processD-ribose catabolic process
C0046835biological_processcarbohydrate phosphorylation
C0046872molecular_functionmetal ion binding
D0004747molecular_functionribokinase activity
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006014biological_processD-ribose metabolic process
D0016301molecular_functionkinase activity
D0019303biological_processD-ribose catabolic process
D0046835biological_processcarbohydrate phosphorylation
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue ADP A 401
ChainResidue
AASN187
ALEU297
ACYS300
AHOH509
AHOH514
ATHR238
ALEU239
AGLY240
AALA241
AGLY243
AILE244
AALA271
AGLY272

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 402
ChainResidue
AASN14
AASP16
AGLY42
ALYS43
AGLU138
AHOH516

site_idAC3
Number of Residues1
Detailsbinding site for residue NA A 403
ChainResidue
AGLU188

site_idAC4
Number of Residues12
Detailsbinding site for residue ADP B 401
ChainResidue
BASN187
BTHR238
BGLY240
BALA241
BGLY243
BILE244
BALA271
BGLY272
BLEU297
BCYS300
BNA403
BHOH511

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO B 402
ChainResidue
BASN14
BASP16
BGLY42
BLYS43
BALA96
BGLU138

site_idAC6
Number of Residues3
Detailsbinding site for residue NA B 403
ChainResidue
BGLU188
BGLY240
BADP401

site_idAC7
Number of Residues9
Detailsbinding site for residue ADP C 400
ChainResidue
CASN187
CTHR238
CGLY240
CGLY243
CILE244
CALA271
CGLY272
CLEU297
CCYS300

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO C 401
ChainResidue
CASN14
CASP16
CGLY42
CASN46
CALA96

site_idAC9
Number of Residues15
Detailsbinding site for residue ADP D 401
ChainResidue
DASN187
DTHR238
DLEU239
DGLY240
DALA241
DGLY243
DILE244
DALA271
DGLY272
DLEU297
DCYS300
DNA402
DHOH501
DHOH505
DHOH507

site_idAD1
Number of Residues1
Detailsbinding site for residue NA D 402
ChainResidue
DADP401

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PDB entries from 2024-06-12

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