Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1YRH

Crystal Structure Of Trp Repressor Binding Protein Wrba in complex with FMN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
A	0008753	molecular_function	NADPH dehydrogenase (quinone) activity
A	0010181	molecular_function	FMN binding
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
B	0000166	molecular_function	nucleotide binding
B	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
B	0008753	molecular_function	NADPH dehydrogenase (quinone) activity
B	0010181	molecular_function	FMN binding
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
C	0000166	molecular_function	nucleotide binding
C	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
C	0008753	molecular_function	NADPH dehydrogenase (quinone) activity
C	0010181	molecular_function	FMN binding
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
D	0000166	molecular_function	nucleotide binding
D	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
D	0008753	molecular_function	NADPH dehydrogenase (quinone) activity
D	0010181	molecular_function	FMN binding
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
E	0000166	molecular_function	nucleotide binding
E	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
E	0008753	molecular_function	NADPH dehydrogenase (quinone) activity
E	0010181	molecular_function	FMN binding
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
F	0000166	molecular_function	nucleotide binding
F	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
F	0008753	molecular_function	NADPH dehydrogenase (quinone) activity
F	0010181	molecular_function	FMN binding
F	0016020	cellular_component	membrane
F	0016491	molecular_function	oxidoreductase activity
F	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
G	0000166	molecular_function	nucleotide binding
G	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
G	0008753	molecular_function	NADPH dehydrogenase (quinone) activity
G	0010181	molecular_function	FMN binding
G	0016020	cellular_component	membrane
G	0016491	molecular_function	oxidoreductase activity
G	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity
H	0000166	molecular_function	nucleotide binding
H	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
H	0008753	molecular_function	NADPH dehydrogenase (quinone) activity
H	0010181	molecular_function	FMN binding
H	0016020	cellular_component	membrane
H	0016491	molecular_function	oxidoreductase activity
H	0050136	molecular_function	NADH dehydrogenase (quinone) (non-electrogenic) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FMN D 401

Chain	Residue
A	HIS142
D	THR86
D	ARG87
D	PHE88
D	SER121
D	ALA122
D	GLN123
D	ASN124
D	GLY127
D	HOH410
B	TYR152
D	SER13
D	SER14
D	THR15
D	GLY16
D	THR17
D	GLY18
D	PRO85

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FMN C 402

Chain	Residue
A	TYR152
B	HIS142
C	SER13
C	SER14
C	THR15
C	GLY16
C	THR17
C	GLY18
C	PRO85
C	THR86
C	ARG87
C	PHE88
C	SER121
C	ALA122
C	GLN123
C	ASN124
C	GLY127
C	ALA171

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE FMN B 403

Chain	Residue
B	SER13
B	SER14
B	THR15
B	GLY16
B	THR17
B	GLY18
B	PRO85
B	THR86
B	ARG87
B	PHE88
B	GLY89
B	SER121
B	ALA122
B	GLN123
B	ASN124
B	GLY127
C	ASP100
C	HIS142
D	TYR152

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE FMN A 404

Chain	Residue
A	SER13
A	SER14
A	THR15
A	GLY16
A	THR17
A	GLY18
A	PRO85
A	THR86
A	ARG87
A	PHE88
A	GLY89
A	SER121
A	ALA122
A	GLN123
A	ASN124
A	GLY127
D	HIS142

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FMN H 405

Chain	Residue
E	HIS142
H	SER13
H	SER14
H	THR15
H	GLY16
H	THR17
H	GLY18
H	PRO85
H	THR86
H	ARG87
H	PHE88
H	GLY89
H	SER121
H	ALA122
H	GLN123
H	ASN124
H	GLY127
H	ALA171

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FMN G 406

Chain	Residue
G	THR86
G	ARG87
G	PHE88
G	SER121
G	ALA122
G	GLN123
G	ASN124
G	GLY127
G	HOH417
E	TYR152
F	HIS142
G	SER13
G	SER14
G	THR15
G	GLY16
G	THR17
G	GLY18
G	PRO85

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE FMN F 407

Chain	Residue
F	SER13
F	SER14
F	THR15
F	GLY16
F	THR17
F	GLY18
F	PRO85
F	THR86
F	ARG87
F	PHE88
F	GLY89
F	SER121
F	ALA122
F	GLN123
F	ASN124
F	GLY127
F	HOH425
G	ASP100
G	HIS142
H	TYR152

site_id	AC8
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FMN E 408

Chain	Residue
E	SER13
E	SER14
E	THR15
E	GLY16
E	THR17
E	GLY18
E	PRO85
E	THR86
E	ARG87
E	PHE88
E	SER121
E	ALA122
E	GLN123
E	ASN124
E	GLY127
G	TYR152
H	ASP100
H	HIS142

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	112
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16322580","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)