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2I5Q

Crystal structure of Apo L-rhamnonate dehydratase from Escherichia Coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009063biological_processamino acid catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0050032molecular_functionL-rhamnonate dehydratase activity
B0000287molecular_functionmagnesium ion binding
B0009063biological_processamino acid catabolic process
B0016052biological_processcarbohydrate catabolic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0050032molecular_functionL-rhamnonate dehydratase activity
Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. TiSCVDlALwDLfGKvvglPVykLLG
ChainResidueDetails
ATHR136-GLY161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01288","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01288","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Increases basicity of active site His","evidences":[{"source":"HAMAP-Rule","id":"MF_01288","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01288","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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