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2ITM

Crystal structure of the E. coli xylulose kinase complexed with xylulose

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004856molecular_functionD-xylulokinase activity
A0005524molecular_functionATP binding
A0005975biological_processcarbohydrate metabolic process
A0005997biological_processxylulose metabolic process
A0005998biological_processxylulose catabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0042732biological_processD-xylose metabolic process
A0042803molecular_functionprotein homodimerization activity
A0042843biological_processD-xylose catabolic process
A0046835biological_processcarbohydrate phosphorylation
A0103020molecular_function1-deoxy-D-xylulose kinase activity
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004856molecular_functionD-xylulokinase activity
B0005524molecular_functionATP binding
B0005975biological_processcarbohydrate metabolic process
B0005997biological_processxylulose metabolic process
B0005998biological_processxylulose catabolic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0042732biological_processD-xylose metabolic process
B0042803molecular_functionprotein homodimerization activity
B0042843biological_processD-xylose catabolic process
B0046835biological_processcarbohydrate phosphorylation
B0103020molecular_function1-deoxy-D-xylulose kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE XUL A 4930
ChainResidue
AMET77
AHIS78
ATRP96
AASP233
AASN234
AMET288

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE XUL B 4931
ChainResidue
BASP233
BASN234
BMET288
BHOH5058
BHOH5113
BHOH5116
BMET77
BHIS78
BTRP96

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 4932
ChainResidue
BGLY254
BTHR255
BGLY394
BGLY395

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 4931
ChainResidue
AARG196
AHOH5150

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NH4 B 4933
ChainResidue
BARG137

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NH4 B 4935
ChainResidue
AASN309
AVAL310
AARG398
BARG54

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NH4 A 4935
ChainResidue
AASP197

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NH4 A 4938
ChainResidue
AVAL33

Functional Information from PROSITE/UniProt
site_idPS00445
Number of Residues21
DetailsFGGY_KINASES_2 FGGY family of carbohydrate kinases signature 2. GvFFGLthqhgpn.ELARAVLE
ChainResidueDetails
AGLY347-GLU367

site_idPS00933
Number of Residues13
DetailsFGGY_KINASES_1 FGGY family of carbohydrate kinases signature 1. GfTapKLLWVQRH
ChainResidueDetails
AGLY126-HIS138

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_02220","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17123542","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02220","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17123542","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Important for activity","evidences":[{"source":"HAMAP-Rule","id":"MF_02220","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17123542","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

240291

PDB entries from 2025-08-13

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