Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8RHP

Cryo-EM structure of the molybdenum nitrogenase complexed with iron protein (NifH) and Shethna protein II (FeSII)

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	0005737	cellular_component	cytoplasm
E	0046872	molecular_function	metal ion binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051537	molecular_function	2 iron, 2 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	0016612	cellular_component	molybdenum-iron nitrogenase complex
H	0046872	molecular_function	metal ion binding
H	0051536	molecular_function	iron-sulfur cluster binding
I	0000166	molecular_function	nucleotide binding
I	0005524	molecular_function	ATP binding
I	0009399	biological_process	nitrogen fixation
I	0016163	molecular_function	nitrogenase activity
I	0016491	molecular_function	oxidoreductase activity
I	0016612	cellular_component	molybdenum-iron nitrogenase complex
I	0046872	molecular_function	metal ion binding
I	0051536	molecular_function	iron-sulfur cluster binding
J	0000166	molecular_function	nucleotide binding
J	0005524	molecular_function	ATP binding
J	0009399	biological_process	nitrogen fixation
J	0016163	molecular_function	nitrogenase activity
J	0016491	molecular_function	oxidoreductase activity
J	0016612	cellular_component	molybdenum-iron nitrogenase complex
J	0046872	molecular_function	metal ion binding
J	0051536	molecular_function	iron-sulfur cluster binding
K	0000166	molecular_function	nucleotide binding
K	0005524	molecular_function	ATP binding
K	0009399	biological_process	nitrogen fixation
K	0016163	molecular_function	nitrogenase activity
K	0016491	molecular_function	oxidoreductase activity
K	0016612	cellular_component	molybdenum-iron nitrogenase complex
K	0046872	molecular_function	metal ion binding
K	0051536	molecular_function	iron-sulfur cluster binding
L	0005737	cellular_component	cytoplasm
L	0046872	molecular_function	metal ion binding
L	0051536	molecular_function	iron-sulfur cluster binding
L	0051537	molecular_function	2 iron, 2 sulfur cluster binding
M	0000166	molecular_function	nucleotide binding
M	0005524	molecular_function	ATP binding
M	0009399	biological_process	nitrogen fixation
M	0016163	molecular_function	nitrogenase activity
M	0016491	molecular_function	oxidoreductase activity
M	0046872	molecular_function	metal ion binding
M	0051536	molecular_function	iron-sulfur cluster binding
M	0051539	molecular_function	4 iron, 4 sulfur cluster binding
N	0000166	molecular_function	nucleotide binding
N	0005524	molecular_function	ATP binding
N	0009399	biological_process	nitrogen fixation
N	0016163	molecular_function	nitrogenase activity
N	0016491	molecular_function	oxidoreductase activity
N	0046872	molecular_function	metal ion binding
N	0051536	molecular_function	iron-sulfur cluster binding
N	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

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CQDGNCGSC

Chain	Residue	Details
E	CYS42-CYS50

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

Chain	Residue	Details
F	ASP126-PRO139

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
F	GLU88-GLY100

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	72
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	234
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	74
Details	Region: {"description":"N-loop","evidences":[{"source":"PubMed","id":"26654855","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26654855","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
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
F	LYS11	electrostatic stabiliser, hydrogen bond donor
F	LYS16	electrostatic stabiliser, hydrogen bond donor
F	LYS42	electrostatic stabiliser, hydrogen bond donor
F	ASP130	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
G	LYS11	electrostatic stabiliser, hydrogen bond donor
G	LYS16	electrostatic stabiliser, hydrogen bond donor
G	LYS42	electrostatic stabiliser, hydrogen bond donor
G	ASP130	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
M	LYS11	electrostatic stabiliser, hydrogen bond donor
M	LYS16	electrostatic stabiliser, hydrogen bond donor
M	LYS42	electrostatic stabiliser, hydrogen bond donor
M	ASP130	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
N	LYS11	electrostatic stabiliser, hydrogen bond donor
N	LYS16	electrostatic stabiliser, hydrogen bond donor
N	LYS42	electrostatic stabiliser, hydrogen bond donor
N	ASP130	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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