Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2CGK

Crystal Structure of L-rhamnulose kinase from Escherichia coli in an open uncomplexed conformation.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008993molecular_functionrhamnulokinase activity
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019299biological_processrhamnose metabolic process
A0019301biological_processrhamnose catabolic process
A0046835biological_processcarbohydrate phosphorylation
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008993molecular_functionrhamnulokinase activity
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0019299biological_processrhamnose metabolic process
B0019301biological_processrhamnose catabolic process
B0046835biological_processcarbohydrate phosphorylation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000269|PubMed:16674975
ChainResidueDetails
AASP237
BASP237

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000269|PubMed:16674975
ChainResidueDetails
AALA13
BHIS236
BTHR259
BASN296
BGLN304
BGLY402
AGLY83
AHIS236
ATHR259
AASN296
AGLN304
AGLY402
BALA13
BGLY83

238268

PDB entries from 2025-07-02

PDB statisticsPDBj update infoContact PDBjnumon