Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5X1Y

Structure of mercuric reductase from Lysinibacillus sphaericus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0016152	molecular_function	mercury (II) reductase (NADP+) activity
A	0016491	molecular_function	oxidoreductase activity
A	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A	0045340	molecular_function	mercury ion binding
A	0046689	biological_process	response to mercury ion
A	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050661	molecular_function	NADP binding
A	0050787	biological_process	detoxification of mercury ion
B	0000166	molecular_function	nucleotide binding
B	0016152	molecular_function	mercury (II) reductase (NADP+) activity
B	0016491	molecular_function	oxidoreductase activity
B	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B	0045340	molecular_function	mercury ion binding
B	0046689	biological_process	response to mercury ion
B	0046872	molecular_function	metal ion binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050661	molecular_function	NADP binding
B	0050787	biological_process	detoxification of mercury ion
C	0000166	molecular_function	nucleotide binding
C	0016152	molecular_function	mercury (II) reductase (NADP+) activity
C	0016491	molecular_function	oxidoreductase activity
C	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
C	0045340	molecular_function	mercury ion binding
C	0046689	biological_process	response to mercury ion
C	0046872	molecular_function	metal ion binding
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0050661	molecular_function	NADP binding
C	0050787	biological_process	detoxification of mercury ion
D	0000166	molecular_function	nucleotide binding
D	0016152	molecular_function	mercury (II) reductase (NADP+) activity
D	0016491	molecular_function	oxidoreductase activity
D	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
D	0045340	molecular_function	mercury ion binding
D	0046689	biological_process	response to mercury ion
D	0046872	molecular_function	metal ion binding
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0050661	molecular_function	NADP binding
D	0050787	biological_process	detoxification of mercury ion
E	0000166	molecular_function	nucleotide binding
E	0016152	molecular_function	mercury (II) reductase (NADP+) activity
E	0016491	molecular_function	oxidoreductase activity
E	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
E	0045340	molecular_function	mercury ion binding
E	0046689	biological_process	response to mercury ion
E	0046872	molecular_function	metal ion binding
E	0050660	molecular_function	flavin adenine dinucleotide binding
E	0050661	molecular_function	NADP binding
E	0050787	biological_process	detoxification of mercury ion
F	0000166	molecular_function	nucleotide binding
F	0016152	molecular_function	mercury (II) reductase (NADP+) activity
F	0016491	molecular_function	oxidoreductase activity
F	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
F	0045340	molecular_function	mercury ion binding
F	0046689	biological_process	response to mercury ion
F	0046872	molecular_function	metal ion binding
F	0050660	molecular_function	flavin adenine dinucleotide binding
F	0050661	molecular_function	NADP binding
F	0050787	biological_process	detoxification of mercury ion

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	binding site for residue FAD B 601

Chain	Residue
B	ILE90
B	GLY120
B	THR121
B	CYS122
B	ILE125
B	GLY126
B	CYS127
B	LYS131
B	GLY193
B	GLU194
B	ALA195
B	GLY91
B	THR219
B	GLY220
B	SER239
B	TYR259
B	ARG347
B	LEU354
B	GLY386
B	ASP387
B	GLN393
B	PHE394
B	GLY93
B	VAL395
B	TYR396
B	ALA398
B	ALA94
B	ALA95
B	ILE113
B	GLU114
B	ARG115
B	GLY116

site_id	AC2
Number of Residues	26
Details	binding site for residue FAD A 601

Chain	Residue
A	ILE90
A	GLY93
A	ALA94
A	ALA95
A	GLU114
A	ARG115
A	GLY116
A	GLY120
A	THR121
A	CYS122
A	CYS127
A	LYS131
A	ALA195
A	THR219
A	GLY220
A	SER239
A	TYR259
A	ARG347
A	LEU354
A	GLY386
A	ASP387
A	GLN393
A	PHE394
A	VAL395
A	TYR396
A	ALA398

site_id	AC3
Number of Residues	26
Details	binding site for residue FAD C 601

Chain	Residue
C	ILE90
C	GLY91
C	GLY93
C	ALA94
C	ALA95
C	GLU114
C	ARG115
C	GLY120
C	THR121
C	CYS122
C	CYS127
C	LYS131
C	ALA195
C	THR219
C	GLY220
C	SER239
C	TYR259
C	ILE260
C	ARG347
C	LEU354
C	GLY386
C	ASP387
C	GLN393
C	PHE394
C	VAL395
C	TYR396

site_id	AC4
Number of Residues	28
Details	binding site for residue FAD D 601

Chain	Residue
D	ALA195
D	THR219
D	GLY220
D	TYR259
D	ARG347
D	LEU354
D	GLY386
D	ASP387
D	GLN393
D	PHE394
D	VAL395
D	TYR396
D	ALA398
D	GLY91
D	GLY93
D	ALA94
D	ALA95
D	ILE113
D	GLU114
D	ARG115
D	GLY120
D	THR121
D	CYS122
D	GLY126
D	CYS127
D	LYS131
D	GLY193
D	GLU194

site_id	AC5
Number of Residues	25
Details	binding site for residue FAD E 601

Chain	Residue
E	ILE90
E	GLY91
E	GLY93
E	ALA94
E	ALA95
E	GLU114
E	ARG115
E	GLY120
E	THR121
E	CYS122
E	GLY126
E	CYS127
E	LYS131
E	ALA195
E	THR219
E	GLY220
E	SER239
E	TYR259
E	ARG347
E	LEU354
E	GLY386
E	ASP387
E	PHE394
E	VAL395
E	TYR396

site_id	AC6
Number of Residues	27
Details	binding site for residue FAD F 601

Chain	Residue
F	ILE90
F	GLY91
F	GLY93
F	ALA94
F	ALA95
F	GLU114
F	ARG115
F	GLY116
F	THR121
F	CYS122
F	GLY126
F	CYS127
F	LYS131
F	GLU194
F	ALA195
F	THR219
F	GLY220
F	TYR259
F	ARG347
F	LEU354
F	GLY386
F	ASP387
F	GLN393
F	PHE394
F	VAL395
F	TYR396
F	PHE427

Functional Information from PROSITE/UniProt

site_id	PS00076
Number of Residues	11
Details	PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVniGCVP

Chain	Residue	Details
B	GLY119-PRO129

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00280

Chain	Residue	Details
B	CYS13
E	CYS16
F	CYS13
F	CYS16
B	CYS16
A	CYS13
A	CYS16
C	CYS13
C	CYS16
D	CYS13
D	CYS16
E	CYS13

site_id	SWS_FT_FI2
Number of Residues	42
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P00392

Chain	Residue	Details
B	ALA96
A	THR121
A	ALA195
A	VAL395
A	CYS543
A	CYS544
C	ALA96
C	GLY116
C	THR121
C	ALA195
C	VAL395
B	GLY116
C	CYS543
C	CYS544
D	ALA96
D	GLY116
D	THR121
D	ALA195
D	VAL395
D	CYS543
D	CYS544
E	ALA96
B	THR121
E	GLY116
E	THR121
E	ALA195
E	VAL395
E	CYS543
E	CYS544
F	ALA96
F	GLY116
F	THR121
F	ALA195
B	ALA195
F	VAL395
F	CYS543
F	CYS544
B	VAL395
B	CYS543
B	CYS544
A	ALA96
A	GLY116

site_id	SWS_FT_FI3
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255\|PIRSR:PIRSR000350-3

Chain	Residue	Details
B	LYS131
C	GLY256
C	GLY346
C	ASP387
D	LYS131
D	GLY256
D	GLY346
D	ASP387
E	LYS131
E	GLY256
E	GLY346
B	GLY256
E	ASP387
F	LYS131
F	GLY256
F	GLY346
F	ASP387
B	GLY346
B	ASP387
A	LYS131
A	GLY256
A	GLY346
A	ASP387
C	LYS131

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