Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7X32

Crystal structure of E. coli NfsB in complex with berberine

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
A	0046256	biological_process	2,4,6-trinitrotoluene catabolic process
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
B	0046256	biological_process	2,4,6-trinitrotoluene catabolic process
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
C	0046256	biological_process	2,4,6-trinitrotoluene catabolic process
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
D	0046256	biological_process	2,4,6-trinitrotoluene catabolic process
E	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
E	0004155	molecular_function	6,7-dihydropteridine reductase activity
E	0005829	cellular_component	cytosol
E	0010181	molecular_function	FMN binding
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0042802	molecular_function	identical protein binding
E	0042803	molecular_function	protein homodimerization activity
E	0046256	biological_process	2,4,6-trinitrotoluene catabolic process
F	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
F	0004155	molecular_function	6,7-dihydropteridine reductase activity
F	0005829	cellular_component	cytosol
F	0010181	molecular_function	FMN binding
F	0016020	cellular_component	membrane
F	0016491	molecular_function	oxidoreductase activity
F	0042802	molecular_function	identical protein binding
F	0042803	molecular_function	protein homodimerization activity
F	0046256	biological_process	2,4,6-trinitrotoluene catabolic process
G	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
G	0004155	molecular_function	6,7-dihydropteridine reductase activity
G	0005829	cellular_component	cytosol
G	0010181	molecular_function	FMN binding
G	0016020	cellular_component	membrane
G	0016491	molecular_function	oxidoreductase activity
G	0042802	molecular_function	identical protein binding
G	0042803	molecular_function	protein homodimerization activity
G	0046256	biological_process	2,4,6-trinitrotoluene catabolic process
H	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
H	0004155	molecular_function	6,7-dihydropteridine reductase activity
H	0005829	cellular_component	cytosol
H	0010181	molecular_function	FMN binding
H	0016020	cellular_component	membrane
H	0016491	molecular_function	oxidoreductase activity
H	0042802	molecular_function	identical protein binding
H	0042803	molecular_function	protein homodimerization activity
H	0046256	biological_process	2,4,6-trinitrotoluene catabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:11020276, ECO:0000269\|PubMed:11491290, ECO:0000269\|PubMed:15684426

Chain	Residue	Details
A	ARG10
D	ARG10
D	GLU165
D	LYS205
E	ARG10
E	GLU165
E	LYS205
F	ARG10
F	GLU165
F	LYS205
G	ARG10
A	GLU165
G	GLU165
G	LYS205
H	ARG10
H	GLU165
H	LYS205
A	LYS205
B	ARG10
B	GLU165
B	LYS205
C	ARG10
C	GLU165
C	LYS205

site_id	SWS_FT_FI2
Number of Residues	40
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q01234

Chain	Residue	Details
A	LYS14
B	ARG107
C	LYS14
C	THR41
C	ASN71
C	LYS74
C	ARG107
D	LYS14
D	THR41
D	ASN71
D	LYS74
A	THR41
D	ARG107
E	LYS14
E	THR41
E	ASN71
E	LYS74
E	ARG107
F	LYS14
F	THR41
F	ASN71
F	LYS74
A	ASN71
F	ARG107
G	LYS14
G	THR41
G	ASN71
G	LYS74
G	ARG107
H	LYS14
H	THR41
H	ASN71
H	LYS74
A	LYS74
H	ARG107
A	ARG107
B	LYS14
B	THR41
B	ASN71
B	LYS74

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

site_id	MCSA5
Number of Residues	3
Details	M-CSA 211

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

site_id	MCSA6
Number of Residues	3
Details	M-CSA 211

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

site_id	MCSA7
Number of Residues	3
Details	M-CSA 211

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

site_id	MCSA8
Number of Residues	3
Details	M-CSA 211

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

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