1KQB

Structure of Nitroreductase from E. cloacae complex with inhibitor benzoate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0016491	molecular_function	oxidoreductase activity
A	0046256	biological_process	2,4,6-trinitrotoluene catabolic process
B	0005829	cellular_component	cytosol
B	0016491	molecular_function	oxidoreductase activity
B	0046256	biological_process	2,4,6-trinitrotoluene catabolic process
C	0005829	cellular_component	cytosol
C	0016491	molecular_function	oxidoreductase activity
C	0046256	biological_process	2,4,6-trinitrotoluene catabolic process
D	0005829	cellular_component	cytosol
D	0016491	molecular_function	oxidoreductase activity
D	0046256	biological_process	2,4,6-trinitrotoluene catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN A 518

Chain	Residue
A	ARG10
A	GLY166
A	LYS205
A	ARG207
A	HOH538
A	HOH554
A	HOH562
A	HOH586
B	PRO38
B	SER39
B	SER40
A	HIS11
B	ASN42
B	LEU145
B	BEZ525
A	SER12
A	LYS14
A	ASN71
A	LYS74
A	PRO163
A	ILE164
A	GLU165

---

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FMN B 519

Chain	Residue
A	PRO38
A	SER39
A	SER40
A	ASN42
A	GLN142
A	LEU145
A	BEZ524
B	ARG10
B	HIS11
B	SER12
B	LYS14
B	ASN71
B	LYS74
B	TYR144
B	PRO163
B	ILE164
B	GLU165
B	GLY166
B	ASN200
B	LYS205
B	ARG207
B	HOH528
B	HOH539
B	HOH544
B	HOH552

---

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE FMN C 520

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	LYS205
C	ARG207
C	HOH536
C	HOH538
C	HOH551
C	HOH555
C	HOH567
D	PRO38
D	SER39
D	SER40
D	ASN42
D	GLN142
D	LEU145
D	BEZ523
D	HOH530

---

site_id	AC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE FMN D 521

Chain	Residue
C	PRO38
C	SER39
C	SER40
C	ASN42
C	GLN142
C	LEU145
C	BEZ522
D	ARG10
D	HIS11
D	SER12
D	LYS14
D	ASN71
D	LYS74
D	TYR144
D	PRO163
D	ILE164
D	GLU165
D	GLY166
D	ASN200
D	LYS205
D	ARG207
D	HOH528
D	HOH531
D	HOH536
D	HOH551
D	HOH556

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BEZ C 522

Chain	Residue
C	SER40
C	THR41
C	PHE124
C	HOH636
D	GLY166
D	FMN521

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BEZ D 523

Chain	Residue
C	GLY166
C	FMN520
D	SER40
D	THR41
D	PHE124

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BEZ A 524

Chain	Residue
A	SER40
A	THR41
A	PHE124
B	PHE70
B	GLY166
B	FMN519

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BEZ B 525

Chain	Residue
A	GLY166
A	FMN518
B	SER40
B	THR41
B	PHE124
B	HOH554

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:28578873, ECO:0007744|PDB:5J8D

Chain	Residue	Details
A	ARG10
D	ARG10
D	GLU165
D	LYS205
A	GLU165
A	LYS205
B	ARG10
B	GLU165
B	LYS205
C	ARG10
C	GLU165
C	LYS205

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000305|PubMed:28578873, ECO:0007744|PDB:5J8D

Chain	Residue	Details
A	LYS14
B	ASN71
B	LYS74
B	ARG107
C	LYS14
C	THR41
C	THR67
C	ASN71
C	LYS74
C	ARG107
D	LYS14
A	THR41
D	THR41
D	THR67
D	ASN71
D	LYS74
D	ARG107
A	THR67
A	ASN71
A	LYS74
A	ARG107
B	LYS14
B	THR41
B	THR67

---