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4BC4

Crystal structure of human D-xylulokinase in complex with D-xylulose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004856molecular_functionD-xylulokinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0005997biological_processxylulose metabolic process
A0005998biological_processxylulose catabolic process
A0006091biological_processgeneration of precursor metabolites and energy
A0016301molecular_functionkinase activity
A0019640biological_processglucuronate catabolic process to xylulose 5-phosphate
A0042732biological_processD-xylose metabolic process
A0046835biological_processcarbohydrate phosphorylation
B0004856molecular_functionD-xylulokinase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0005997biological_processxylulose metabolic process
B0005998biological_processxylulose catabolic process
B0006091biological_processgeneration of precursor metabolites and energy
B0016301molecular_functionkinase activity
B0019640biological_processglucuronate catabolic process to xylulose 5-phosphate
B0042732biological_processD-xylose metabolic process
B0046835biological_processcarbohydrate phosphorylation
C0004856molecular_functionD-xylulokinase activity
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0005997biological_processxylulose metabolic process
C0005998biological_processxylulose catabolic process
C0006091biological_processgeneration of precursor metabolites and energy
C0016301molecular_functionkinase activity
C0019640biological_processglucuronate catabolic process to xylulose 5-phosphate
C0042732biological_processD-xylose metabolic process
C0046835biological_processcarbohydrate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue XUL A 1532
ChainResidue
AGLN97
AGLN98
AHIS99
ATRP137
AARG170
AASP280
AASN281
AHOH2007

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 1533
ChainResidue
ACYS252
APRO324
AVAL325
AASP326
ASER327
ASER251

site_idAC3
Number of Residues8
Detailsbinding site for residue XUL B 1531
ChainResidue
BGLN97
BGLN98
BHIS99
BTRP137
BARG170
BASP280
BASN281
BHOH2008

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO B 1532
ChainResidue
BILE131
BASP133
BLYS178
BHOH2065
BHOH2093

site_idAC5
Number of Residues8
Detailsbinding site for residue XUL C 1531
ChainResidue
CGLN97
CGLN98
CHIS99
CTRP137
CARG170
CASP280
CASN281
CHOH2007

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO C 1532
ChainResidue
CSER251
CCYS252
CPRO324
CVAL325
CASP326
CSER327
CHOH2227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsBINDING:
ChainResidueDetails
AASN281
ATRP355
AGLY441
AASN445
BHIS99
BARG170
BASP280
BASN281
BTRP355
BGLY441
BASN445
CHIS99
CARG170
CASP280
CASN281
CTRP355
CGLY441
CASN445
AHIS99
AARG170
AASP280

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PDB entries from 2024-05-29

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