Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4WZA

Asymmetric Nucleotide Binding in the Nitrogenase Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0009399	biological_process	nitrogen fixation
A	0016163	molecular_function	nitrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016612	cellular_component	molybdenum-iron nitrogenase complex
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0009399	biological_process	nitrogen fixation
B	0016163	molecular_function	nitrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0016612	cellular_component	molybdenum-iron nitrogenase complex
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0009399	biological_process	nitrogen fixation
C	0016163	molecular_function	nitrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016612	cellular_component	molybdenum-iron nitrogenase complex
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0009399	biological_process	nitrogen fixation
D	0016163	molecular_function	nitrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016612	cellular_component	molybdenum-iron nitrogenase complex
D	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
E	0000166	molecular_function	nucleotide binding
E	0005524	molecular_function	ATP binding
E	0009399	biological_process	nitrogen fixation
E	0016163	molecular_function	nitrogenase activity
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
F	0000166	molecular_function	nucleotide binding
F	0005524	molecular_function	ATP binding
F	0009399	biological_process	nitrogen fixation
F	0016163	molecular_function	nitrogenase activity
F	0016491	molecular_function	oxidoreductase activity
F	0046872	molecular_function	metal ion binding
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0000166	molecular_function	nucleotide binding
G	0005524	molecular_function	ATP binding
G	0009399	biological_process	nitrogen fixation
G	0016163	molecular_function	nitrogenase activity
G	0016491	molecular_function	oxidoreductase activity
G	0046872	molecular_function	metal ion binding
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051539	molecular_function	4 iron, 4 sulfur cluster binding
H	0000166	molecular_function	nucleotide binding
H	0005524	molecular_function	ATP binding
H	0009399	biological_process	nitrogen fixation
H	0016163	molecular_function	nitrogenase activity
H	0016491	molecular_function	oxidoreductase activity
H	0046872	molecular_function	metal ion binding
H	0051536	molecular_function	iron-sulfur cluster binding
H	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue HCA A 1494

Chain	Residue
A	ALA65
A	HOH1572
A	HOH1582
A	HOH1587
A	HOH1588
A	HOH1778
B	HOH1528
B	HOH1653
A	GLN191
A	GLY424
A	ILE425
A	HIS442
A	ICS1496
A	HOH1507
A	HOH1519
A	HOH1532

site_id	AC2
Number of Residues	12
Details	binding site for residue ICS A 1496

Chain	Residue
A	VAL70
A	ARG96
A	HIS195
A	TYR229
A	CYS275
A	GLY356
A	GLY357
A	LEU358
A	ARG359
A	PHE381
A	HIS442
A	HCA1494

site_id	AC3
Number of Residues	14
Details	binding site for residue CLF A 1498

Chain	Residue
A	CYS62
A	TYR64
A	PRO85
A	GLY87
A	CYS88
A	TYR91
A	CYS154
A	GLY185
B	CYS70
B	SER92
B	CYS95
B	TYR98
B	CYS153
B	SER188

site_id	AC4
Number of Residues	6
Details	binding site for residue FE B 1492

Chain	Residue
B	ARG108
B	GLU109
B	HOH1629
D	ASP353
D	ASP357
D	HOH1970

site_id	AC5
Number of Residues	16
Details	binding site for residue HCA C 1494

Chain	Residue
C	ALA65
C	GLN191
C	GLY424
C	ILE425
C	HIS442
C	ICS1496
C	HOH1522
C	HOH1530
C	HOH1562
C	HOH1591
C	HOH1594
C	HOH1595
C	HOH1605
D	HOH1560
D	HOH1617
D	HOH1619

site_id	AC6
Number of Residues	12
Details	binding site for residue ICS C 1496

Chain	Residue
C	VAL70
C	ARG96
C	HIS195
C	TYR229
C	CYS275
C	GLY356
C	GLY357
C	LEU358
C	ARG359
C	PHE381
C	HIS442
C	HCA1494

site_id	AC7
Number of Residues	14
Details	binding site for residue CLF C 1498

Chain	Residue
C	CYS62
C	TYR64
C	PRO85
C	GLY87
C	CYS88
C	TYR91
C	CYS154
C	GLY185
D	CYS70
D	SER92
D	CYS95
D	TYR98
D	CYS153
D	SER188

site_id	AC8
Number of Residues	6
Details	binding site for residue FE D 1492

Chain	Residue
B	ASP353
B	ASP357
B	HOH1618
D	ARG108
D	GLU109
D	HOH1935

site_id	AC9
Number of Residues	9
Details	binding site for residue SF4 E 1290

Chain	Residue
E	GLY99
E	CYS132
F	CYS97
F	ALA98
F	GLY99
F	CYS132
A	LEU158
B	VAL157
E	CYS97

site_id	AD1
Number of Residues	6
Details	binding site for residue MG E 1291

Chain	Residue
E	SER16
E	ADP1292
E	HOH1317
E	HOH1318
E	HOH1319
E	HOH1320

site_id	AD2
Number of Residues	19
Details	binding site for residue ADP E 1292

Chain	Residue
E	LYS10
E	GLY12
E	ILE13
E	GLY14
E	LYS15
E	SER16
E	THR17
E	ASN185
E	VAL211
E	PRO212
E	ARG213
E	ASP214
E	VAL217
E	GLU221
E	GLN236
E	MG1291
E	HOH1319
E	HOH1320
F	MET156

site_id	AD3
Number of Residues	5
Details	binding site for residue MG F 1291

Chain	Residue
F	SER16
F	ACP1292
F	HOH1310
F	HOH1311
F	HOH1312

site_id	AD4
Number of Residues	23
Details	binding site for residue ACP F 1292

Chain	Residue
E	MET156
F	GLY11
F	GLY12
F	ILE13
F	GLY14
F	LYS15
F	SER16
F	THR17
F	ASP39
F	LYS41
F	GLY128
F	ASN185
F	PRO212
F	ARG213
F	ASP214
F	VAL217
F	GLN218
F	GLU221
F	GLN236
F	MG1291
F	HOH1311
F	HOH1312
F	HOH1382

site_id	AD5
Number of Residues	8
Details	binding site for residue SF4 G 1290

Chain	Residue
C	LEU158
D	VAL157
G	CYS97
G	GLY99
G	CYS132
H	CYS97
H	GLY99
H	CYS132

site_id	AD6
Number of Residues	7
Details	binding site for residue MG G 1291

Chain	Residue
G	SER16
G	ASP39
G	ADP1292
G	HOH1318
G	HOH1319
G	HOH1320
G	HOH1321

site_id	AD7
Number of Residues	19
Details	binding site for residue ADP G 1292

Chain	Residue
G	LYS10
G	GLY12
G	ILE13
G	GLY14
G	LYS15
G	SER16
G	THR17
G	ASN185
G	PRO212
G	ARG213
G	ASP214
G	VAL217
G	GLN218
G	GLU221
G	GLN236
G	MG1291
G	HOH1320
G	HOH1321
G	HOH1371

site_id	AD8
Number of Residues	5
Details	binding site for residue MG H 1291

Chain	Residue
H	SER16
H	ACP1292
H	HOH1315
H	HOH1316
H	HOH1317

site_id	AD9
Number of Residues	25
Details	binding site for residue ACP H 1292

Chain	Residue
G	LYS10
G	MET156
G	HOH1377
H	GLY11
H	GLY12
H	ILE13
H	GLY14
H	LYS15
H	SER16
H	THR17
H	ASP39
H	LYS41
H	GLY128
H	ASN185
H	PRO212
H	ARG213
H	ASP214
H	VAL217
H	GLN218
H	GLU221
H	GLN236
H	MG1291
H	HOH1316
H	HOH1317
H	HOH1392

Functional Information from PROSITE/UniProt

site_id	PS00090
Number of Residues	15
Details	NITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. SECpigliGDDIeSV

Chain	Residue	Details
A	SER152-VAL166
B	THR151-PHE165

site_id	PS00692
Number of Residues	14
Details	NIFH_FRXC_2 NifH/frxC family signature 2. DvLGDVVCGGFAmP

Chain	Residue	Details
E	ASP125-PRO138

site_id	PS00699
Number of Residues	8
Details	NITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. ISHGPVGC

Chain	Residue	Details
A	ILE81-CYS88
B	TYR88-CYS95

site_id	PS00746
Number of Residues	13
Details	NIFH_FRXC_1 NifH/frxC family signature 1. EsGGPepGvGCAG

Chain	Residue	Details
E	GLU87-GLY99

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	54
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
E	LYS10	electrostatic stabiliser, hydrogen bond donor
E	LYS15	electrostatic stabiliser, hydrogen bond donor
E	LYS41	electrostatic stabiliser, hydrogen bond donor
E	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
F	LYS10	electrostatic stabiliser, hydrogen bond donor
F	LYS15	electrostatic stabiliser, hydrogen bond donor
F	LYS41	electrostatic stabiliser, hydrogen bond donor
F	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
G	LYS10	electrostatic stabiliser, hydrogen bond donor
G	LYS15	electrostatic stabiliser, hydrogen bond donor
G	LYS41	electrostatic stabiliser, hydrogen bond donor
G	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
H	LYS10	electrostatic stabiliser, hydrogen bond donor
H	LYS15	electrostatic stabiliser, hydrogen bond donor
H	LYS41	electrostatic stabiliser, hydrogen bond donor
H	ASP129	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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