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2FWM

Crystal Structure of E. coli EntA, a 2,3-dihydrodihydroxy benzoate dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
X0005515molecular_functionprotein binding
X0005829cellular_componentcytosol
X0008667molecular_function2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase activity
X0009239biological_processenterobactin biosynthetic process
X0016491molecular_functionoxidoreductase activity
X0019290biological_processsiderophore biosynthetic process
X0032991cellular_componentprotein-containing complex
X0042802molecular_functionidentical protein binding
Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SdaahtprigMsaYGASKAALkSLAlSVG
ChainResidueDetails
XSER131-GLY159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues25
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
XLYS148
XSER131
XTYR144

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
XASN103
XLYS148
XSER131
XTYR144

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
XLYS148
XMET141

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
XLYS148
XTYR144

242842

PDB entries from 2025-10-08

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