Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1YKI

The structure of E. coli nitroreductase bound with the antibiotic nitrofurazone

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	23
Details	BINDING SITE FOR RESIDUE FMN A 1218

Chain	Residue
A	ARG10
A	GLY166
A	LYS205
A	ARG207
A	NFZ1219
A	HOH1229
A	HOH1232
A	HOH1233
A	HOH1266
B	PRO38
B	SER39
A	HIS11
B	SER40
B	ASN42
B	GLN142
B	LEU145
A	SER12
A	LYS14
A	ASN71
A	LYS74
A	PRO163
A	ILE164
A	GLU165

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NFZ A 1219

Chain	Residue
A	ASN67
A	TYR68
A	PHE70
A	ASN71
A	GLU165
A	FMN1218
A	HOH1251
A	HOH1421
B	THR41
B	PHE124

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FMN B 2218

Chain	Residue
A	PRO38
A	SER39
A	SER40
A	ASN42
A	GLN142
A	LEU145
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	NFZ2219
B	HOH2229
B	HOH2237
B	HOH2239
B	HOH2256

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NFZ B 2219

Chain	Residue
A	THR41
A	PHE124
B	ASN67
B	TYR68
B	PHE70
B	ASN71
B	LYS74
B	GLU165
B	FMN2218
B	HOH2290
B	HOH2342

site_id	AC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FMN C 3218

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	NFZ3219
C	HOH4222
C	HOH4233
C	HOH4234
C	HOH4241
D	PRO38
D	SER39
D	SER40
D	ASN42
D	GLN142
D	LEU145

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NFZ C 3219

Chain	Residue
C	HOH4275
C	HOH4289
D	THR41
D	PHE124
C	ASN67
C	TYR68
C	PHE70
C	ASN71
C	GLU165
C	FMN3218
C	CIT4220

site_id	AC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN D 4218

Chain	Residue
C	PRO38
C	SER39
C	SER40
C	ASN42
C	GLN142
C	LEU145
D	ARG10
D	HIS11
D	SER12
D	LYS14
D	ASN71
D	LYS74
D	PRO163
D	ILE164
D	GLU165
D	GLY166
D	LYS205
D	ARG207
D	NFZ4219
D	HOH4231
D	HOH4236
D	HOH4252
D	HOH4261

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NFZ D 4219

Chain	Residue
C	THR41
C	PHE124
D	ASN67
D	TYR68
D	PHE70
D	ASN71
D	GLU165
D	FMN4218
D	HOH4281
D	HOH4301

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT C 4220

Chain	Residue
C	LYS14
C	LYS74
C	PHE199
C	NFZ3219
C	HOH4275
C	HOH4279
C	HOH4307
D	ASN117

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS C 1223

Chain	Residue
C	LYS9
C	ALA201
C	LEU203

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS C 1224

Chain	Residue
D	SER52
D	HOH4274
D	HOH4295

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMS B 1225

Chain	Residue
B	ALA104
B	ASP105

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

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

Chain

Residue

Details

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

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