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_FI2
Number of Residues	56
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_FI3
Number of Residues	40
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

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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

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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

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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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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

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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

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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

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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

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