2R96

Crystal structure of E. coli 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	0005829	cellular_component	cytosol
A	0006979	biological_process	response to oxidative stress
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	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0050136	molecular_function	NADH:ubiquinone reductase (non-electrogenic) activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
C	0000166	molecular_function	nucleotide binding
C	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
C	0005829	cellular_component	cytosol
C	0006979	biological_process	response to oxidative stress
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	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0050136	molecular_function	NADH:ubiquinone reductase (non-electrogenic) activity
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN A 198

Chain	Residue
A	SER9
A	PHE79
A	SER112
A	THR113
A	GLY114
A	GLY116
A	GLY117
A	TYR142
A	EDO204
A	HOH208
A	HOH224
A	MET10
C	ASP91
C	HIS132
C	EDO204
A	TYR11
A	GLY12
A	HIS13
A	ILE14
A	PRO76
A	THR77
A	ARG78

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 199

Chain	Residue
A	ALA143
A	ALA144
A	GLN145
A	GLU146

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 200

Chain	Residue
A	THR41
A	GLY84
A	GLN85
A	HOH231
C	THR88
C	ASP91

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 201

Chain	Residue
A	LEU191
A	LYS194
C	GLU48

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 202

Chain	Residue
A	ARG37
A	GLU40
A	THR54
A	GLN55

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 203

Chain	Residue
A	TRP97
A	HOH247
C	FMN198
C	EDO199

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 204

Chain	Residue
A	GLY114
A	THR115
A	FMN198
C	TRP97
C	EDO204

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 205

Chain	Residue
A	ALA22
A	SER26
A	VAL33

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 206

Chain	Residue
A	TYR183
A	GLU186
A	TYR187
A	HOH239

---

site_id	BC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN C 198

Chain	Residue
A	ASP91
A	HIS132
A	EDO203
C	SER9
C	MET10
C	TYR11
C	GLY12
C	HIS13
C	ILE14
C	PRO76
C	THR77
C	ARG78
C	PHE79
C	SER112
C	THR113
C	GLY114
C	THR115
C	GLY117
C	TYR142
C	EDO199
C	HOH214
C	HOH232

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 199

Chain	Residue
A	EDO203
C	GLY114
C	THR115
C	FMN198

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 200

Chain	Residue
C	LYS2
C	GLU32
C	ASP67

---

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 201

Chain	Residue
C	TYR7
C	TYR8
C	SER9
C	ARG37
C	VAL38
C	GLN55

---

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 202

Chain	Residue
C	TYR11
C	GLY12
C	HIS13
C	THR16
C	GLN172
C	PRO173

---

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 203

Chain	Residue
C	ARG171
C	GLN172

---

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 204

Chain	Residue
A	EDO204
C	TRP97
C	HOH242
A	FMN198

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000269|PubMed:17951395, ECO:0000269|PubMed:19665595

Chain	Residue	Details
A	SER9
A	THR77
A	SER112
A	HIS132
C	SER9
C	THR77
C	SER112
C	HIS132

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:17951395

Chain	Residue	Details
A	TYR11
A	ALA50
A	ASP168
C	TYR11
C	ALA50
C	ASP168

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000305|PubMed:17951395

Chain	Residue	Details
A	TRP97
C	TRP97

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	LYS49
C	LYS49

---