1ICU

THE STRUCTURE OF ESCHERICHIA COLI NITROREDUCTASE COMPLEXED WITH NICOTINIC ACID

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
A	0004155	molecular_function	6,7-dihydropteridine reductase activity
A	0005829	cellular_component	cytosol
A	0010181	molecular_function	FMN binding
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
B	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
B	0004155	molecular_function	6,7-dihydropteridine reductase activity
B	0005829	cellular_component	cytosol
B	0010181	molecular_function	FMN binding
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
C	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
C	0004155	molecular_function	6,7-dihydropteridine reductase activity
C	0005829	cellular_component	cytosol
C	0010181	molecular_function	FMN binding
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
D	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
D	0004155	molecular_function	6,7-dihydropteridine reductase activity
D	0005829	cellular_component	cytosol
D	0010181	molecular_function	FMN binding
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN A 218

Chain	Residue
A	ARG10
A	GLY166
A	ASN200
A	LYS205
A	ARG207
A	HOH227
A	HOH241
A	HOH242
B	PRO38
B	SER39
B	SER40
A	HIS11
B	ASN42
B	LEU145
B	NIO219
A	SER12
A	LYS14
A	ASN71
A	LYS74
A	PRO163
A	ILE164
A	GLU165

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NIO B 219

Chain	Residue
A	PHE70
A	GLY166
A	FMN218
B	SER40
B	THR41
B	PHE124

---

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN B 220

Chain	Residue
A	PRO38
A	SER39
A	SER40
A	ASN42
A	GLN142
A	LEU145
A	NIO221
B	ARG10
B	HIS11
B	SER12
B	LYS14
B	ASN71
B	LYS74
B	PRO163
B	ILE164
B	GLU165
B	GLY166
B	ASN200
B	LYS205
B	ARG207
B	HOH226
B	HOH241
B	HOH248

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NIO A 221

Chain	Residue
A	SER40
A	THR41
A	PHE124
B	PHE70
B	GLY166
B	FMN220

---

site_id	AC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FMN C 222

Chain	Residue
C	ARG10
C	HIS11
C	SER12
C	LYS14
C	ASN71
C	LYS74
C	TYR144
C	PRO163
C	ILE164
C	GLU165
C	GLY166
C	ASN200
C	LYS205
C	ARG207
C	HOH234
C	HOH237
C	HOH242
D	PRO38
D	SER39
D	SER40
D	ASN42
D	GLN142
D	LEU145
D	NIO223

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NIO D 223

Chain	Residue
C	PHE70
C	GLY166
C	FMN222
D	SER40
D	THR41
D	PHE124

---

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE FMN D 224

Chain	Residue
D	PRO163
D	ILE164
D	GLU165
D	GLY166
D	LYS205
D	ARG207
D	HOH237
D	HOH239
D	HOH250
C	PRO38
C	SER39
C	SER40
C	ASN42
C	LEU145
C	NIO225
D	ARG10
D	HIS11
D	SER12
D	LYS14
D	ASN71
D	LYS74

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NIO C 225

Chain	Residue
C	SER40
C	THR41
C	PHE124
D	FMN224

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11020276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11491290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15684426","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q01234","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 211

Chain	Residue	Details
A	LYS14	electrostatic stabiliser, hydrogen bond donor
A	LYS74	electrostatic stabiliser, hydrogen bond donor
A	GLU165	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 211

Chain	Residue	Details
B	LYS14	electrostatic stabiliser, hydrogen bond donor
B	LYS74	electrostatic stabiliser, hydrogen bond donor
B	GLU165	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA3
Number of Residues	3
Details	M-CSA 211

Chain	Residue	Details
C	LYS14	electrostatic stabiliser, hydrogen bond donor
C	LYS74	electrostatic stabiliser, hydrogen bond donor
C	GLU165	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA4
Number of Residues	3
Details	M-CSA 211

Chain	Residue	Details
D	LYS14	electrostatic stabiliser, hydrogen bond donor
D	LYS74	electrostatic stabiliser, hydrogen bond donor
D	GLU165	electrostatic stabiliser, hydrogen bond donor

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