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8BPP

crystal structure of N-ethylmaleimide reductase (nemA) from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006805biological_processxenobiotic metabolic process
A0008748molecular_functionN-ethylmaleimide reductase activity
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016628molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
A0018937biological_processnitroglycerin metabolic process
A0046256biological_process2,4,6-trinitrotoluene catabolic process
A0046857molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor
B0005829cellular_componentcytosol
B0006805biological_processxenobiotic metabolic process
B0008748molecular_functionN-ethylmaleimide reductase activity
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0016628molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
B0018937biological_processnitroglycerin metabolic process
B0046256biological_process2,4,6-trinitrotoluene catabolic process
B0046857molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor
C0005829cellular_componentcytosol
C0006805biological_processxenobiotic metabolic process
C0008748molecular_functionN-ethylmaleimide reductase activity
C0010181molecular_functionFMN binding
C0016491molecular_functionoxidoreductase activity
C0016628molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
C0018937biological_processnitroglycerin metabolic process
C0046256biological_process2,4,6-trinitrotoluene catabolic process
C0046857molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P42593
ChainResidueDetails
ATYR187
BTYR187
CTYR187

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P42593
ChainResidueDetails
AGLN101
AARG234
AGLY324
BGLN101
BARG234
BGLY324
CGLN101
CARG234
CGLY324

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PDB entries from 2025-06-18

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