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1F5V

STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS. ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE AMINO ACID SUBSTITUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0034567molecular_functionchromate reductase activity
A0042803molecular_functionprotein homodimerization activity
B0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0034567molecular_functionchromate reductase activity
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN A 360
ChainResidue
AHIS11
ALYS167
AARG169
AHOH367
AHOH380
AHOH403
AHOH475
BSER38
BSER39
BSER40
BPHE42
ASER13
BVAL106
BASP107
BHOH504
AARG15
AGLN67
AVAL127
ATYR128
AILE129
AGLY130
AGLY131

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN B 361
ChainResidue
ASER38
ASER39
ASER40
APHE42
AVAL106
AASP107
BHIS11
BARG12
BSER13
BARG15
BGLN67
BVAL127
BTYR128
BILE129
BGLY130
BGLY131
BLYS167
BARG169
BHOH381
BHOH416
BHOH425
BHOH427
BHOH498

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:11034992, ECO:0007744|PDB:1F5V
ChainResidueDetails
AHIS11
BLYS167
ASER39
AGLN67
ATYR128
ALYS167
BHIS11
BSER39
BGLN67
BTYR128

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PDB entries from 2024-07-17

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