8DFC

CryoEM structure of the 1:1 ADP-tetrafluoroaluminate stabilized nitrogenase complex from Azotobacter vinelandii

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

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

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

Chain	Residue	Details
E	ASP125-PRO138

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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

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

Chain	Residue	Details
E	GLU87-GLY99

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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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

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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

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