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3RH7

Crystal structure of a putative oxidoreductase (SMa0793) from Sinorhizobium meliloti 1021 at 3.00 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016646molecular_functionoxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
A0042602molecular_functionriboflavin reductase (NADPH) activity
B0000166molecular_functionnucleotide binding
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0016646molecular_functionoxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
B0042602molecular_functionriboflavin reductase (NADPH) activity
C0000166molecular_functionnucleotide binding
C0010181molecular_functionFMN binding
C0016491molecular_functionoxidoreductase activity
C0016646molecular_functionoxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
C0042602molecular_functionriboflavin reductase (NADPH) activity
D0000166molecular_functionnucleotide binding
D0010181molecular_functionFMN binding
D0016491molecular_functionoxidoreductase activity
D0016646molecular_functionoxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
D0042602molecular_functionriboflavin reductase (NADPH) activity
E0000166molecular_functionnucleotide binding
E0010181molecular_functionFMN binding
E0016491molecular_functionoxidoreductase activity
E0016646molecular_functionoxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
E0042602molecular_functionriboflavin reductase (NADPH) activity
F0000166molecular_functionnucleotide binding
F0010181molecular_functionFMN binding
F0016491molecular_functionoxidoreductase activity
F0016646molecular_functionoxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
F0042602molecular_functionriboflavin reductase (NADPH) activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FMN A 321
ChainResidue
APHE37
AARG61
AASN62
APHE88
AALA89
AARG95
AILE286
AGLY287
AASN288
ATHR38
AALA39
AASN40
ASER41
ACYS55
ALEU56
AALA57
ASER60

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FMN C 321
ChainResidue
CPHE37
CTHR38
CALA39
CASN40
CSER41
CCYS55
CLEU56
CALA57
CSER60
CARG61
CASN62
CPHE88
CALA89
CARG95
CTYR151
CILE286
CGLY287
CASN288

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FMN D 321
ChainResidue
DPHE37
DTHR38
DALA39
DASN40
DSER41
DCYS55
DLEU56
DALA57
DSER60
DARG61
DASN62
DPHE88
DALA89
DARG95
DTYR151
DILE286
DGLY287
DASN288

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FMN F 321
ChainResidue
FPHE37
FTHR38
FALA39
FASN40
FSER41
FCYS55
FLEU56
FALA57
FSER60
FARG61
FASN62
FPHE88
FALA89
FARG95
FTYR151
FILE286
FGLY287
FASN288

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues66
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"APR-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of a hypothetical oxidoreductase (SMa0793) from Sinorhizobium meliloti 1021 at 3.00 A resolution.","authoringGroup":["Joint Center for Structural Genomics (JCSG)"]}},{"source":"PDB","id":"3RH7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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