Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1R27

Crystal Structure of NarGH complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0008940	molecular_function	nitrate reductase activity
A	0009055	molecular_function	electron transfer activity
A	0009061	biological_process	anaerobic respiration
A	0009325	cellular_component	nitrate reductase complex
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0019645	biological_process	anaerobic electron transport chain
A	0042126	biological_process	nitrate metabolic process
A	0043546	molecular_function	molybdopterin cofactor binding
A	0044799	cellular_component	NarGHI complex
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	0160182	molecular_function	nitrate reductase (quinone) activity
B	0005515	molecular_function	protein binding
B	0005886	cellular_component	plasma membrane
B	0008940	molecular_function	nitrate reductase activity
B	0009055	molecular_function	electron transfer activity
B	0009061	biological_process	anaerobic respiration
B	0009325	cellular_component	nitrate reductase complex
B	0016020	cellular_component	membrane
B	0019645	biological_process	anaerobic electron transport chain
B	0042126	biological_process	nitrate metabolic process
B	0044799	cellular_component	NarGHI complex
B	0051538	molecular_function	3 iron, 4 sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0160182	molecular_function	nitrate reductase (quinone) activity
C	0005515	molecular_function	protein binding
C	0005886	cellular_component	plasma membrane
C	0008940	molecular_function	nitrate reductase activity
C	0009055	molecular_function	electron transfer activity
C	0009061	biological_process	anaerobic respiration
C	0009325	cellular_component	nitrate reductase complex
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0019645	biological_process	anaerobic electron transport chain
C	0042126	biological_process	nitrate metabolic process
C	0043546	molecular_function	molybdopterin cofactor binding
C	0044799	cellular_component	NarGHI complex
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0160182	molecular_function	nitrate reductase (quinone) activity
D	0005515	molecular_function	protein binding
D	0005886	cellular_component	plasma membrane
D	0008940	molecular_function	nitrate reductase activity
D	0009055	molecular_function	electron transfer activity
D	0009061	biological_process	anaerobic respiration
D	0009325	cellular_component	nitrate reductase complex
D	0016020	cellular_component	membrane
D	0019645	biological_process	anaerobic electron transport chain
D	0042126	biological_process	nitrate metabolic process
D	0044799	cellular_component	NarGHI complex
D	0051538	molecular_function	3 iron, 4 sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0160182	molecular_function	nitrate reductase (quinone) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MO A 5803

Chain	Residue
A	ASP222
A	MGD5801
A	MGD5802
A	HOH6570

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MO C 7803

Chain	Residue
C	ASP222
C	MGD7801
C	MGD7802
C	HOH8538

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE F3S B 5808

Chain	Residue
B	ILE201
B	CYS217
B	ARG218
B	TRP220
B	ARG221
B	MET222
B	CYS223
B	SER241
B	CYS196

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE F3S D 7808

Chain	Residue
D	CYS196
D	ILE201
D	CYS217
D	ARG218
D	TRP220
D	ARG221
D	MET222
D	CYS223
D	SER241

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 5800

Chain	Residue
B	CYS26
B	ASN42
B	CYS244
B	ILE245
B	PHE246
B	CYS247
B	THR257
B	CYS259

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 5805

Chain	Residue
B	CYS184
B	GLU185
B	CYS187
B	ALA191
B	CYS192
B	CYS227
B	TYR229
B	ILE232
B	LYS243

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 5806

Chain	Residue
B	CYS16
B	GLY18
B	CYS19
B	HIS20
B	CYS22
B	CYS263
B	GLY265
B	ILE267
B	ARG268

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 A 5807

Chain	Residue
A	HIS49
A	VAL51
A	CYS53
A	GLY55
A	SER56
A	CYS57
A	TRP59
A	GLY91
A	CYS92
A	TYR1101

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 D 7800

Chain	Residue
D	CYS26
D	TRP30
D	ASN42
D	CYS244
D	ILE245
D	PHE246
D	CYS247
D	THR257
D	CYS259

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 D 7805

Chain	Residue
D	CYS184
D	GLU185
D	CYS187
D	ALA191
D	CYS192
D	CYS227
D	TYR229
D	ILE232
D	LYS243

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 D 7806

Chain	Residue
D	CYS16
D	CYS19
D	HIS20
D	CYS22
D	CYS263
D	VAL264
D	GLY265
D	ILE267
D	ARG268

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 C 7807

Chain	Residue
C	TYR1101
C	HIS49
C	VAL51
C	CYS53
C	GLY55
C	SER56
C	CYS57
C	TRP59
C	GLY91
C	CYS92
C	GLY95

site_id	BC4
Number of Residues	40
Details	BINDING SITE FOR RESIDUE MGD A 5801

Chain	Residue
A	GLY50
A	ASN52
A	PRO190
A	TYR220
A	ASP222
A	HIS546
A	TRP712
A	ARG713
A	SER714
A	ASN715
A	SER720
A	LYS722
A	LEU771
A	ASP772
A	PHE773
A	ARG774
A	THR788
A	TRP791
A	LYS794
A	ASP822
A	THR1090
A	HIS1092
A	ILE1097
A	HIS1098
A	SER1099
A	THR1100
A	HIS1163
A	ASN1185
A	ASN1217
A	ARG1218
A	MGD5802
A	MO5803
A	HOH5995
A	HOH6018
A	HOH6058
A	HOH6090
A	HOH6135
A	HOH6568
A	HOH6570
A	HOH6580

site_id	BC5
Number of Residues	39
Details	BINDING SITE FOR RESIDUE MGD A 5802

Chain	Residue
A	ASN52
A	ARG94
A	ASP222
A	TRP252
A	GLY253
A	ASN255
A	GLN258
A	THR259
A	VAL280
A	THR281
A	PRO282
A	ASP283
A	ALA285
A	GLN299
A	GLY300
A	ASP302
A	GLY541
A	ALA542
A	GLY543
A	LEU544
A	TRP547
A	TYR577
A	VAL578
A	GLY579
A	PRO1091
A	HIS1092
A	GLN1093
A	GLY1096
A	ILE1097
A	HIS1098
A	ARG1218
A	MGD5801
A	MO5803
A	HOH5875
A	HOH5889
A	HOH5923
A	HOH6075
A	HOH6577
A	HOH6615

site_id	BC6
Number of Residues	38
Details	BINDING SITE FOR RESIDUE MGD C 7801

Chain	Residue
C	GLY50
C	ASN52
C	PRO190
C	TYR220
C	ASP222
C	HIS546
C	ARG713
C	SER714
C	ASN715
C	SER720
C	LYS722
C	LEU771
C	ASP772
C	PHE773
C	ARG774
C	THR788
C	TRP791
C	LYS794
C	ASP822
C	THR1090
C	HIS1092
C	ILE1097
C	HIS1098
C	SER1099
C	THR1100
C	HIS1163
C	HIS1184
C	ASN1185
C	ASN1217
C	ARG1218
C	MGD7802
C	MO7803
C	HOH7861
C	HOH7908
C	HOH8037
C	HOH8108
C	HOH8538
C	HOH8539

site_id	BC7
Number of Residues	38
Details	BINDING SITE FOR RESIDUE MGD C 7802

Chain	Residue
C	ASN52
C	ARG94
C	ASP222
C	TRP252
C	GLY253
C	ASN255
C	GLN258
C	THR259
C	VAL280
C	THR281
C	PRO282
C	ASP283
C	ALA285
C	GLN299
C	GLY300
C	ASP302
C	GLY541
C	ALA542
C	GLY543
C	LEU544
C	TRP547
C	TYR577
C	VAL578
C	GLY579
C	PRO1091
C	HIS1092
C	GLN1093
C	GLY1096
C	ILE1097
C	HIS1098
C	ARG1218
C	MGD7801
C	MO7803
C	HOH7833
C	HOH7865
C	HOH7970
C	HOH8022
C	HOH8129

Functional Information from PROSITE/UniProt

site_id	PS00490
Number of Residues	18
Details	MOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. SsTClySDIILPtATwyE

Chain	Residue	Details
A	SER776-GLU793

site_id	PS00551
Number of Residues	19
Details	MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. StHgvnCTGsCsWkIyvk.N

Chain	Residue	Details
A	SER47-ASN65

site_id	PS00932
Number of Residues	28
Details	MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AkdlGIaDnDwIeVfNsnGaltarAvVS

Chain	Residue	Details
A	ALA1124-SER1151

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	128
Details	Domain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01004","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	56
Details	Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	62
Details	Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	58
Details	Domain: {"description":"4Fe-4S ferredoxin-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12910261","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14725769","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	CYS213

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

Chain	Residue	Details
C	CYS213

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)