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4YZE

Crystal structure of E.coli NemR reduced form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003700molecular_functionDNA-binding transcription factor activity
A0005515molecular_functionprotein binding
A0009889biological_processregulation of biosynthetic process
A0045892biological_processnegative regulation of DNA-templated transcription
A0080090biological_processregulation of primary metabolic process
B0003677molecular_functionDNA binding
B0003700molecular_functionDNA-binding transcription factor activity
B0005515molecular_functionprotein binding
B0009889biological_processregulation of biosynthetic process
B0045892biological_processnegative regulation of DNA-templated transcription
B0080090biological_processregulation of primary metabolic process
C0003677molecular_functionDNA binding
C0003700molecular_functionDNA-binding transcription factor activity
C0005515molecular_functionprotein binding
C0009889biological_processregulation of biosynthetic process
C0045892biological_processnegative regulation of DNA-templated transcription
C0080090biological_processregulation of primary metabolic process
D0003677molecular_functionDNA binding
D0003700molecular_functionDNA-binding transcription factor activity
D0005515molecular_functionprotein binding
D0009889biological_processregulation of biosynthetic process
D0045892biological_processnegative regulation of DNA-templated transcription
D0080090biological_processregulation of primary metabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues76
DetailsDNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00335
ChainResidueDetails
AGLY30-PHE49
BGLY30-PHE49
CGLY30-PHE49
DGLY30-PHE49

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Plays a central role in response to RCS => ECO:0000269|PubMed:23536188, ECO:0000269|PubMed:25867078
ChainResidueDetails
ACYS106
BCYS106
CCYS106
DCYS106

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PDB entries from 2024-05-01

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