Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1OGY

Crystal structure of the heterodimeric nitrate reductase from Rhodobacter sphaeroides

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0006777	biological_process	Mo-molybdopterin cofactor biosynthetic process
A	0008940	molecular_function	nitrate reductase activity
A	0009055	molecular_function	electron transfer activity
A	0009325	cellular_component	nitrate reductase complex
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0030151	molecular_function	molybdenum ion binding
A	0042128	biological_process	nitrate assimilation
A	0042597	cellular_component	periplasmic space
A	0043546	molecular_function	molybdopterin cofactor binding
A	0045333	biological_process	cellular respiration
A	0046872	molecular_function	metal ion binding
A	0050140	molecular_function	nitrate reductase (cytochrome) activity
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	1990204	cellular_component	oxidoreductase complex
B	0009061	biological_process	anaerobic respiration
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
C	0005506	molecular_function	iron ion binding
C	0006777	biological_process	Mo-molybdopterin cofactor biosynthetic process
C	0008940	molecular_function	nitrate reductase activity
C	0009055	molecular_function	electron transfer activity
C	0009325	cellular_component	nitrate reductase complex
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0030151	molecular_function	molybdenum ion binding
C	0042128	biological_process	nitrate assimilation
C	0042597	cellular_component	periplasmic space
C	0043546	molecular_function	molybdopterin cofactor binding
C	0045333	biological_process	cellular respiration
C	0046872	molecular_function	metal ion binding
C	0050140	molecular_function	nitrate reductase (cytochrome) activity
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	1990204	cellular_component	oxidoreductase complex
D	0009061	biological_process	anaerobic respiration
D	0042597	cellular_component	periplasmic space
D	0046872	molecular_function	metal ion binding
E	0005506	molecular_function	iron ion binding
E	0006777	biological_process	Mo-molybdopterin cofactor biosynthetic process
E	0008940	molecular_function	nitrate reductase activity
E	0009055	molecular_function	electron transfer activity
E	0009325	cellular_component	nitrate reductase complex
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0030151	molecular_function	molybdenum ion binding
E	0042128	biological_process	nitrate assimilation
E	0042597	cellular_component	periplasmic space
E	0043546	molecular_function	molybdopterin cofactor binding
E	0045333	biological_process	cellular respiration
E	0046872	molecular_function	metal ion binding
E	0050140	molecular_function	nitrate reductase (cytochrome) activity
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	1990204	cellular_component	oxidoreductase complex
F	0009061	biological_process	anaerobic respiration
F	0042597	cellular_component	periplasmic space
F	0046872	molecular_function	metal ion binding
G	0005506	molecular_function	iron ion binding
G	0006777	biological_process	Mo-molybdopterin cofactor biosynthetic process
G	0008940	molecular_function	nitrate reductase activity
G	0009055	molecular_function	electron transfer activity
G	0009325	cellular_component	nitrate reductase complex
G	0016020	cellular_component	membrane
G	0016491	molecular_function	oxidoreductase activity
G	0030151	molecular_function	molybdenum ion binding
G	0042128	biological_process	nitrate assimilation
G	0042597	cellular_component	periplasmic space
G	0043546	molecular_function	molybdopterin cofactor binding
G	0045333	biological_process	cellular respiration
G	0046872	molecular_function	metal ion binding
G	0050140	molecular_function	nitrate reductase (cytochrome) activity
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	1990204	cellular_component	oxidoreductase complex
H	0009061	biological_process	anaerobic respiration
H	0042597	cellular_component	periplasmic space
H	0046872	molecular_function	metal ion binding
I	0005506	molecular_function	iron ion binding
I	0006777	biological_process	Mo-molybdopterin cofactor biosynthetic process
I	0008940	molecular_function	nitrate reductase activity
I	0009055	molecular_function	electron transfer activity
I	0009325	cellular_component	nitrate reductase complex
I	0016020	cellular_component	membrane
I	0016491	molecular_function	oxidoreductase activity
I	0030151	molecular_function	molybdenum ion binding
I	0042128	biological_process	nitrate assimilation
I	0042597	cellular_component	periplasmic space
I	0043546	molecular_function	molybdopterin cofactor binding
I	0045333	biological_process	cellular respiration
I	0046872	molecular_function	metal ion binding
I	0050140	molecular_function	nitrate reductase (cytochrome) activity
I	0051536	molecular_function	iron-sulfur cluster binding
I	0051539	molecular_function	4 iron, 4 sulfur cluster binding
I	1990204	cellular_component	oxidoreductase complex
J	0009061	biological_process	anaerobic respiration
J	0042597	cellular_component	periplasmic space
J	0046872	molecular_function	metal ion binding
K	0005506	molecular_function	iron ion binding
K	0006777	biological_process	Mo-molybdopterin cofactor biosynthetic process
K	0008940	molecular_function	nitrate reductase activity
K	0009055	molecular_function	electron transfer activity
K	0009325	cellular_component	nitrate reductase complex
K	0016020	cellular_component	membrane
K	0016491	molecular_function	oxidoreductase activity
K	0030151	molecular_function	molybdenum ion binding
K	0042128	biological_process	nitrate assimilation
K	0042597	cellular_component	periplasmic space
K	0043546	molecular_function	molybdopterin cofactor binding
K	0045333	biological_process	cellular respiration
K	0046872	molecular_function	metal ion binding
K	0050140	molecular_function	nitrate reductase (cytochrome) activity
K	0051536	molecular_function	iron-sulfur cluster binding
K	0051539	molecular_function	4 iron, 4 sulfur cluster binding
K	1990204	cellular_component	oxidoreductase complex
L	0009061	biological_process	anaerobic respiration
L	0042597	cellular_component	periplasmic space
L	0046872	molecular_function	metal ion binding
M	0005506	molecular_function	iron ion binding
M	0006777	biological_process	Mo-molybdopterin cofactor biosynthetic process
M	0008940	molecular_function	nitrate reductase activity
M	0009055	molecular_function	electron transfer activity
M	0009325	cellular_component	nitrate reductase complex
M	0016020	cellular_component	membrane
M	0016491	molecular_function	oxidoreductase activity
M	0030151	molecular_function	molybdenum ion binding
M	0042128	biological_process	nitrate assimilation
M	0042597	cellular_component	periplasmic space
M	0043546	molecular_function	molybdopterin cofactor binding
M	0045333	biological_process	cellular respiration
M	0046872	molecular_function	metal ion binding
M	0050140	molecular_function	nitrate reductase (cytochrome) activity
M	0051536	molecular_function	iron-sulfur cluster binding
M	0051539	molecular_function	4 iron, 4 sulfur cluster binding
M	1990204	cellular_component	oxidoreductase complex
N	0009061	biological_process	anaerobic respiration
N	0042597	cellular_component	periplasmic space
N	0046872	molecular_function	metal ion binding
O	0005506	molecular_function	iron ion binding
O	0006777	biological_process	Mo-molybdopterin cofactor biosynthetic process
O	0008940	molecular_function	nitrate reductase activity
O	0009055	molecular_function	electron transfer activity
O	0009325	cellular_component	nitrate reductase complex
O	0016020	cellular_component	membrane
O	0016491	molecular_function	oxidoreductase activity
O	0030151	molecular_function	molybdenum ion binding
O	0042128	biological_process	nitrate assimilation
O	0042597	cellular_component	periplasmic space
O	0043546	molecular_function	molybdopterin cofactor binding
O	0045333	biological_process	cellular respiration
O	0046872	molecular_function	metal ion binding
O	0050140	molecular_function	nitrate reductase (cytochrome) activity
O	0051536	molecular_function	iron-sulfur cluster binding
O	0051539	molecular_function	4 iron, 4 sulfur cluster binding
O	1990204	cellular_component	oxidoreductase complex
P	0009061	biological_process	anaerobic respiration
P	0042597	cellular_component	periplasmic space
P	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SF4 A1801

Chain	Residue
A	CYS19
A	CYS22
A	CYS26
A	CYS54
A	GLY57
A	PRO194

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MO A1802

Chain	Residue
A	CYS152
A	MGD1803
A	MGD1804

site_id	AC3
Number of Residues	31
Details	BINDING SITE FOR RESIDUE MGD A1803

Chain	Residue
A	ARG20
A	GLN123
A	ASN148
A	CYS152
A	GLN350
A	GLN384
A	VAL454
A	ASN455
A	ASN456
A	ASN457
A	ALA460
A	SER482
A	ASP483
A	THR487
A	ALA499
A	ALA500
A	MET501
A	LYS505
A	ASP532
A	THR692
A	ARG694
A	TRP699
A	HIS700
A	SER701
A	SER703
A	TRP768
A	ASN776
A	PHE792
A	LYS793
A	MO1802
A	MGD1804

site_id	AC4
Number of Residues	31
Details	BINDING SITE FOR RESIDUE MGD A1804

Chain	Residue
A	LYS56
A	CYS152
A	TRP185
A	GLY186
A	SER187
A	ASN188
A	GLU191
A	MET192
A	SER216
A	THR217
A	HIS220
A	PHE232
A	GLY235
A	ASP237
A	THR345
A	MET346
A	GLY347
A	PHE348
A	GLY383
A	GLN384
A	GLY693
A	ARG694
A	VAL695
A	LEU696
A	HIS698
A	TRP699
A	HIS700
A	LYS793
A	LYS794
A	MO1802
A	MGD1803

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEC B1128

Chain	Residue
B	ARG30
B	PRO40
B	VAL41
B	ILE42
B	PRO43
B	HIS44
B	TYR49
B	ARG57
B	CYS58
B	CYS61
B	HIS62
B	CYS98
B	HIS102

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC B1129

Chain	Residue
B	PHE97
B	CYS98
B	CYS101
B	HIS102
F	ARG64
F	ILE77
A	LEU52
A	ASN53
A	TYR58
B	ARG33
B	TYR35
B	PRO36
B	GLU37
B	GLN38
B	PRO40
B	HIS62
B	MET74
B	ILE75
B	HIS79
B	ARG95
B	TYR96

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 C1801

Chain	Residue
C	CYS19
C	CYS22
C	CYS26
C	ASN53
C	CYS54
C	GLY57
C	PRO194

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MO C1802

Chain	Residue
C	CYS152
C	MGD1803
C	MGD1804

site_id	AC9
Number of Residues	32
Details	BINDING SITE FOR RESIDUE MGD C1803

Chain	Residue
C	ARG20
C	GLN123
C	ASN148
C	CYS152
C	MET346
C	GLN350
C	GLN384
C	VAL454
C	ASN455
C	ASN456
C	ASN457
C	ALA460
C	SER482
C	ASP483
C	THR487
C	ALA499
C	ALA500
C	MET501
C	LYS505
C	ASP532
C	THR692
C	ARG694
C	TRP699
C	HIS700
C	SER701
C	SER703
C	TRP768
C	ASN776
C	PHE792
C	LYS793
C	MO1802
C	MGD1804

site_id	BC1
Number of Residues	30
Details	BINDING SITE FOR RESIDUE MGD C1804

Chain	Residue
C	LYS56
C	CYS152
C	TRP185
C	GLY186
C	ASN188
C	GLU191
C	MET192
C	SER216
C	THR217
C	HIS220
C	PHE232
C	GLY235
C	ASP237
C	THR345
C	MET346
C	GLY347
C	PHE348
C	GLY383
C	GLN384
C	GLY693
C	ARG694
C	VAL695
C	LEU696
C	HIS698
C	TRP699
C	HIS700
C	LYS793
C	LYS794
C	MO1802
C	MGD1803

site_id	BC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEC D1128

Chain	Residue
D	ARG30
D	PRO40
D	VAL41
D	ILE42
D	PRO43
D	HIS44
D	TYR49
D	CYS58
D	CYS61
D	HIS62
D	CYS98
D	HEC1129

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC D1129

Chain	Residue
C	LEU52
C	ASN53
C	TYR58
D	ARG33
D	TYR35
D	PRO36
D	GLU37
D	GLN38
D	PRO40
D	HIS62
D	MET74
D	ILE75
D	HIS79
D	ARG95
D	PHE97
D	CYS98
D	CYS101
D	HIS102
D	HEC1128
H	ARG64
H	ILE77

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SF4 E1801

Chain	Residue
E	CYS19
E	CYS22
E	CYS26
E	CYS54
E	GLY57
E	PRO194

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MO E1802

Chain	Residue
E	CYS152
E	MGD1803
E	MGD1804

site_id	BC6
Number of Residues	31
Details	BINDING SITE FOR RESIDUE MGD E1803

Chain	Residue
E	ARG20
E	GLN123
E	ASN148
E	CYS152
E	MET346
E	GLN350
E	GLN384
E	VAL454
E	ASN455
E	ASN456
E	ALA460
E	SER482
E	ASP483
E	THR487
E	ALA499
E	ALA500
E	MET501
E	LYS505
E	ASP532
E	THR692
E	ARG694
E	TRP699
E	HIS700
E	SER701
E	SER703
E	TRP768
E	ASN776
E	PHE792
E	LYS793
E	MO1802
E	MGD1804

site_id	BC7
Number of Residues	30
Details	BINDING SITE FOR RESIDUE MGD E1804

Chain	Residue
E	LYS56
E	CYS152
E	TRP185
E	GLY186
E	ASN188
E	GLU191
E	MET192
E	SER216
E	THR217
E	HIS220
E	PHE232
E	GLY235
E	ASP237
E	THR345
E	MET346
E	GLY347
E	PHE348
E	GLY383
E	GLN384
E	GLY693
E	ARG694
E	VAL695
E	LEU696
E	HIS698
E	TRP699
E	HIS700
E	LYS793
E	LYS794
E	MO1802
E	MGD1803

site_id	BC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEC F1128

Chain	Residue
F	ARG30
F	VAL41
F	ILE42
F	PRO43
F	HIS44
F	TYR49
F	ARG57
F	CYS58
F	CYS61
F	HIS62
F	HEC1129

site_id	BC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC F1129

Chain	Residue
B	ARG64
B	TYR66
B	ILE77
E	LEU52
E	ASN53
E	TYR58
F	ARG33
F	TYR35
F	PRO36
F	GLU37
F	GLN38
F	PRO40
F	HIS62
F	MET74
F	ILE75
F	HIS79
F	ARG95
F	PHE97
F	CYS98
F	CYS101
F	HIS102
F	HEC1128

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SF4 G1801

Chain	Residue
G	CYS19
G	CYS22
G	CYS26
G	CYS54
G	PRO194

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MO G1802

Chain	Residue
G	CYS152
G	MGD1803
G	MGD1804

site_id	CC3
Number of Residues	32
Details	BINDING SITE FOR RESIDUE MGD G1803

Chain	Residue
G	ARG20
G	GLN123
G	ASN148
G	CYS152
G	MET346
G	GLN350
G	GLN384
G	VAL454
G	ASN455
G	ASN456
G	ASN457
G	ALA460
G	SER482
G	ASP483
G	THR487
G	ALA499
G	ALA500
G	MET501
G	LYS505
G	ASP532
G	THR692
G	ARG694
G	TRP699
G	HIS700
G	SER701
G	SER703
G	TRP768
G	ASN776
G	PHE792
G	LYS793
G	MO1802
G	MGD1804

site_id	CC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE MGD G1804

Chain	Residue
G	LYS56
G	CYS152
G	TRP185
G	GLY186
G	SER187
G	ASN188
G	GLU191
G	MET192
G	SER216
G	THR217
G	HIS220
G	GLY235
G	ASP237
G	THR345
G	MET346
G	GLY347
G	PHE348
G	GLY383
G	GLN384
G	GLY693
G	ARG694
G	VAL695
G	LEU696
G	HIS698
G	TRP699
G	HIS700
G	LYS793
G	LYS794
G	MO1802
G	MGD1803

site_id	CC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEC H1128

Chain	Residue
H	ARG30
H	ARG33
H	PRO40
H	VAL41
H	ILE42
H	PRO43
H	HIS44
H	TYR49
H	ARG57
H	CYS58
H	CYS61
H	HIS62
H	HIS102
H	HEC1129

site_id	CC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC H1129

Chain	Residue
D	ARG64
D	TYR66
D	ILE77
G	LEU52
G	ASN53
G	TYR58
H	ARG33
H	TYR35
H	PRO36
H	GLU37
H	GLN38
H	PRO40
H	HIS62
H	MET74
H	ILE75
H	HIS79
H	ARG95
H	CYS98
H	CYS101
H	HIS102
H	HEC1128

site_id	CC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 I1801

Chain	Residue
I	CYS19
I	PHE21
I	CYS22
I	GLY25
I	CYS26
I	CYS54
I	PRO194

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MO I1802

Chain	Residue
I	CYS152
I	MGD1803
I	MGD1804

site_id	CC9
Number of Residues	32
Details	BINDING SITE FOR RESIDUE MGD I1803

Chain	Residue
I	ARG20
I	GLN123
I	ASN148
I	CYS152
I	MET346
I	GLN350
I	GLN384
I	VAL454
I	ASN455
I	ASN456
I	ASN457
I	ALA460
I	SER482
I	ASP483
I	THR487
I	ALA499
I	ALA500
I	MET501
I	LYS505
I	ASP532
I	THR692
I	ARG694
I	TRP699
I	HIS700
I	SER701
I	SER703
I	TRP768
I	ASN776
I	PHE792
I	LYS793
I	MO1802
I	MGD1804

site_id	DC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE MGD I1804

Chain	Residue
I	LYS56
I	CYS152
I	TRP185
I	GLY186
I	SER187
I	ASN188
I	GLU191
I	MET192
I	SER216
I	THR217
I	HIS220
I	PHE232
I	GLY235
I	ASP237
I	THR345
I	MET346
I	GLY347
I	PHE348
I	GLY383
I	GLN384
I	GLY693
I	ARG694
I	VAL695
I	LEU696
I	HIS698
I	TRP699
I	HIS700
I	LYS793
I	LYS794
I	MO1802
I	MGD1803

site_id	DC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEC J1128

Chain	Residue
J	ARG30
J	ARG33
J	PRO40
J	VAL41
J	ILE42
J	PRO43
J	HIS44
J	TYR49
J	ARG57
J	CYS58
J	CYS61
J	HIS62
J	HEC1129

site_id	DC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEC J1129

Chain	Residue
I	LEU52
I	TYR58
J	ARG33
J	TYR35
J	PRO36
J	GLU37
J	GLN38
J	PRO40
J	LEU59
J	HIS62
J	MET74
J	ILE75
J	SER76
J	HIS79
J	ARG95
J	PHE97
J	CYS98
J	CYS101
J	HIS102
J	HEC1128
P	ARG64
P	TYR66
P	ILE77

site_id	DC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SF4 K1801

Chain	Residue
K	CYS19
K	CYS22
K	CYS26
K	CYS54
K	GLY57
K	PRO194

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MO K1802

Chain	Residue
K	CYS152
K	MGD1803
K	MGD1804

site_id	DC6
Number of Residues	31
Details	BINDING SITE FOR RESIDUE MGD K1803

Chain	Residue
K	ARG20
K	GLN123
K	ASN148
K	CYS152
K	GLN350
K	GLN384
K	VAL454
K	ASN455
K	ASN456
K	ASN457
K	ALA460
K	SER482
K	ASP483
K	THR487
K	ALA499
K	ALA500
K	MET501
K	LYS505
K	ASP532
K	THR692
K	ARG694
K	TRP699
K	HIS700
K	SER701
K	SER703
K	TRP768
K	ASN776
K	PHE792
K	LYS793
K	MO1802
K	MGD1804

site_id	DC7
Number of Residues	31
Details	BINDING SITE FOR RESIDUE MGD K1804

Chain	Residue
K	LYS56
K	CYS152
K	TRP185
K	GLY186
K	SER187
K	ASN188
K	GLU191
K	MET192
K	SER216
K	THR217
K	HIS220
K	PHE232
K	GLY235
K	ASP237
K	THR345
K	MET346
K	GLY347
K	PHE348
K	GLY383
K	GLN384
K	GLY693
K	ARG694
K	VAL695
K	LEU696
K	HIS698
K	TRP699
K	HIS700
K	LYS793
K	LYS794
K	MO1802
K	MGD1803

site_id	DC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEC L1128

Chain	Residue
L	ARG30
L	ARG33
L	PRO40
L	VAL41
L	ILE42
L	PRO43
L	HIS44
L	TYR49
L	ARG57
L	CYS58
L	CYS61
L	HIS62
L	HIS102
L	HEC1129

site_id	DC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC L1129

Chain	Residue
K	LEU52
K	ASN53
K	TYR58
L	ARG33
L	TYR35
L	PRO36
L	GLU37
L	GLN38
L	PRO40
L	HIS62
L	MET74
L	ILE75
L	HIS79
L	ARG95
L	PHE97
L	CYS98
L	CYS101
L	HIS102
L	HEC1128
N	ARG64
N	TYR66
N	ILE77

site_id	EC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SF4 M1801

Chain	Residue
M	CYS19
M	CYS22
M	CYS26
M	CYS54
M	GLY57
M	PRO194

site_id	EC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MO M1802

Chain	Residue
M	CYS152
M	MGD1803
M	MGD1804

site_id	EC3
Number of Residues	32
Details	BINDING SITE FOR RESIDUE MGD M1803

Chain	Residue
M	ARG20
M	GLN123
M	ASN148
M	CYS152
M	MET346
M	GLN350
M	GLN384
M	VAL454
M	ASN455
M	ASN456
M	ASN457
M	ALA460
M	SER482
M	ASP483
M	THR487
M	ALA499
M	ALA500
M	MET501
M	LYS505
M	ASP532
M	THR692
M	ARG694
M	TRP699
M	HIS700
M	SER701
M	SER703
M	TRP768
M	ASN776
M	PHE792
M	LYS793
M	MO1802
M	MGD1804

site_id	EC4
Number of Residues	31
Details	BINDING SITE FOR RESIDUE MGD M1804

Chain	Residue
M	LYS56
M	CYS152
M	TRP185
M	GLY186
M	SER187
M	ASN188
M	GLU191
M	MET192
M	SER216
M	THR217
M	HIS220
M	PHE232
M	GLY235
M	ASP237
M	THR345
M	MET346
M	GLY347
M	PHE348
M	GLY383
M	GLN384
M	GLY693
M	ARG694
M	VAL695
M	LEU696
M	HIS698
M	TRP699
M	HIS700
M	LYS793
M	LYS794
M	MO1802
M	MGD1803

site_id	EC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEC N1128

Chain	Residue
N	ARG30
N	ARG33
N	PRO40
N	VAL41
N	ILE42
N	PRO43
N	HIS44
N	TYR49
N	ARG57
N	CYS58
N	CYS61
N	HIS62
N	HIS102
N	HEC1129

site_id	EC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEC N1129

Chain	Residue
L	ARG64
L	ILE77
M	LEU52
M	ASN53
M	TYR58
N	ARG33
N	PRO36
N	GLU37
N	GLN38
N	PRO40
N	HIS62
N	MET74
N	ILE75
N	HIS79
N	ARG95
N	PHE97
N	CYS98
N	CYS101
N	HIS102
N	HEC1128

site_id	EC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 O1801

Chain	Residue
O	CYS19
O	CYS22
O	CYS26
O	ASN53
O	CYS54
O	GLY57
O	PRO194

site_id	EC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MO O1802

Chain	Residue
O	CYS152
O	MGD1803
O	MGD1804

site_id	EC9
Number of Residues	32
Details	BINDING SITE FOR RESIDUE MGD O1803

Chain	Residue
O	ARG20
O	GLN123
O	ASN148
O	CYS152
O	MET346
O	GLN350
O	GLN384
O	VAL454
O	ASN455
O	ASN456
O	ASN457
O	ALA460
O	SER482
O	ASP483
O	THR487
O	ALA499
O	ALA500
O	MET501
O	LYS505
O	ASP532
O	THR692
O	ARG694
O	TRP699
O	HIS700
O	SER701
O	SER703
O	TRP768
O	ASN776
O	PHE792
O	LYS793
O	MO1802
O	MGD1804

site_id	FC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE MGD O1804

Chain	Residue
O	LYS56
O	CYS152
O	TRP185
O	GLY186
O	SER187
O	ASN188
O	GLU191
O	MET192
O	SER216
O	THR217
O	HIS220
O	PHE232
O	GLY235
O	ASP237
O	THR345
O	MET346
O	GLY347
O	PHE348
O	GLY383
O	GLN384
O	GLY693
O	ARG694
O	VAL695
O	LEU696
O	HIS698
O	TRP699
O	HIS700
O	LYS793
O	LYS794
O	MO1802
O	MGD1803

site_id	FC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEC P1128

Chain	Residue
P	ARG30
P	ARG33
P	VAL41
P	ILE42
P	PRO43
P	HIS44
P	TYR49
P	ARG57
P	CYS58
P	CYS61
P	HIS62
P	CYS98
P	HIS102
P	HEC1129

site_id	FC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC P1129

Chain	Residue
J	ARG64
J	TYR66
J	ILE77
O	LEU52
O	ASN53
O	TYR58
P	ARG33
P	TYR35
P	PRO36
P	GLU37
P	GLN38
P	PRO40
P	HIS62
P	MET74
P	ILE75
P	HIS79
P	ARG95
P	PHE97
P	CYS98
P	CYS101
P	HIS102
P	HEC1128

Functional Information from PROSITE/UniProt

site_id	PS00551
Number of Residues	18
Details	MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. ApCrf.CGTgCgVmVgtr.D

Chain	Residue	Details
A	ALA17-ASP34

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	448
Details	Domain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"HAMAP-Rule","id":"MF_01630","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	272
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01630","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14528294","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OGY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P39185","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01630","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01630","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	32
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	32
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"14528294","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1tmo

Chain	Residue	Details
A	CYS152

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1tmo

Chain	Residue	Details
C	CYS152

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1tmo

Chain	Residue	Details
E	CYS152

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1tmo

Chain	Residue	Details
G	CYS152

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1tmo

Chain	Residue	Details
I	CYS152

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1tmo

Chain	Residue	Details
K	CYS152

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1tmo

Chain	Residue	Details
M	CYS152

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 1tmo

Chain	Residue	Details
O	CYS152

site_id	MCSA1
Number of Residues	6
Details	M-CSA 276

Chain	Residue	Details
A	LYS56	activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
A	CYS152	activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile
A	MET153	electrostatic stabiliser, polar/non-polar interaction, steric role
A	MET346	electrostatic stabiliser, polar/non-polar interaction, steric role
A	GLY383	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
A	GLN384	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA2
Number of Residues	6
Details	M-CSA 276

Chain	Residue	Details
C	LYS56	activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
C	CYS152	activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile
C	MET153	electrostatic stabiliser, polar/non-polar interaction, steric role
C	MET346	electrostatic stabiliser, polar/non-polar interaction, steric role
C	GLY383	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
C	GLN384	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA3
Number of Residues	6
Details	M-CSA 276

Chain	Residue	Details
E	LYS56	activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
E	CYS152	activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile
E	MET153	electrostatic stabiliser, polar/non-polar interaction, steric role
E	MET346	electrostatic stabiliser, polar/non-polar interaction, steric role
E	GLY383	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
E	GLN384	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA4
Number of Residues	6
Details	M-CSA 276

Chain	Residue	Details
G	LYS56	activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
G	CYS152	activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile
G	MET153	electrostatic stabiliser, polar/non-polar interaction, steric role
G	MET346	electrostatic stabiliser, polar/non-polar interaction, steric role
G	GLY383	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
G	GLN384	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA5
Number of Residues	6
Details	M-CSA 276

Chain	Residue	Details
I	LYS56	activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
I	CYS152	activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile
I	MET153	electrostatic stabiliser, polar/non-polar interaction, steric role
I	MET346	electrostatic stabiliser, polar/non-polar interaction, steric role
I	GLY383	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
I	GLN384	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA6
Number of Residues	6
Details	M-CSA 276

Chain	Residue	Details
K	LYS56	activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
K	CYS152	activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile
K	MET153	electrostatic stabiliser, polar/non-polar interaction, steric role
K	MET346	electrostatic stabiliser, polar/non-polar interaction, steric role
K	GLY383	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
K	GLN384	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA7
Number of Residues	6
Details	M-CSA 276

Chain	Residue	Details
M	LYS56	activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
M	CYS152	activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile
M	MET153	electrostatic stabiliser, polar/non-polar interaction, steric role
M	MET346	electrostatic stabiliser, polar/non-polar interaction, steric role
M	GLY383	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
M	GLN384	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA8
Number of Residues	6
Details	M-CSA 276

Chain	Residue	Details
O	LYS56	activator, hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
O	CYS152	activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile
O	MET153	electrostatic stabiliser, polar/non-polar interaction, steric role
O	MET346	electrostatic stabiliser, polar/non-polar interaction, steric role
O	GLY383	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
O	GLN384	electrostatic stabiliser, hydrogen bond acceptor

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