Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1FP6

THE NITROGENASE FE PROTEIN FROM AZOTOBACTER VINELANDII COMPLEXED WITH MGADP

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0046872	molecular_function	metal ion binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster 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	0046872	molecular_function	metal ion binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster 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	0046872	molecular_function	metal ion binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster 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	0046872	molecular_function	metal ion binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 5292

Chain	Residue
A	SER16
A	ADP5291
A	HOH5436
A	HOH5447
A	HOH5457
A	HOH5504

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 6292

Chain	Residue
B	HOH6439
B	HOH6450
B	HOH6483
B	SER16
B	ADP6291
B	HOH6433

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 7292

Chain	Residue
C	SER16
C	ADP7291
C	HOH7450
C	HOH7453
C	HOH7490
C	HOH7504

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG D 8292

Chain	Residue
D	SER16
D	ASP43
D	ADP8291
D	HOH8401
D	HOH8402
D	HOH8415
D	HOH8433

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SF4 A 5290

Chain	Residue
A	CYS97
A	CYS132
B	CYS97
B	ALA98
B	CYS132

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 C 7290

Chain	Residue
C	CYS97
C	CYS132
C	GLY133
D	CYS97
D	ALA98
D	CYS132
D	GLY133

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP A 5291

Chain	Residue
A	GLY12
A	ILE13
A	GLY14
A	LYS15
A	SER16
A	THR17
A	ASN185
A	PRO212
A	ARG213
A	ASP214
A	VAL217
A	GLN218
A	GLU221
A	GLN236
A	MG5292
A	HOH5301
A	HOH5350
A	HOH5408
A	HOH5436
A	HOH5447
A	HOH5457

site_id	AC8
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ADP B 6291

Chain	Residue
B	LYS10
B	GLY12
B	ILE13
B	GLY14
B	LYS15
B	SER16
B	THR17
B	ASN185
B	PRO212
B	ARG213
B	ASP214
B	GLN218
B	GLU221
B	GLN236
B	TYR240
B	MG6292
B	HOH6318
B	HOH6325
B	HOH6376
B	HOH6433
B	HOH6447
B	HOH6450
B	HOH6470
B	HOH6483

site_id	AC9
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP C 7291

Chain	Residue
C	HOH7305
C	HOH7418
C	HOH7422
C	HOH7429
C	HOH7441
C	HOH7453
C	HOH7490
C	HOH7504
C	HOH7536
C	LYS10
C	GLY12
C	ILE13
C	GLY14
C	LYS15
C	SER16
C	THR17
C	ASN185
C	VAL211
C	PRO212
C	ARG213
C	ASP214
C	GLN218
C	GLU221
C	GLN236
C	TYR240
C	MG7292

site_id	BC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ADP D 8291

Chain	Residue
D	GLY12
D	ILE13
D	GLY14
D	LYS15
D	SER16
D	THR17
D	ASN185
D	PRO212
D	ARG213
D	ASP214
D	VAL217
D	GLN218
D	GLU221
D	GLN236
D	MG8292
D	HOH8327
D	HOH8401
D	HOH8415
D	HOH8433
D	HOH8448

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP125-PRO138

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

Chain	Residue	Details
A	GLU87-GLY99

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	LYS10
D	LYS10
D	ALA98
D	GLY133
A	ALA98
A	GLY133
B	LYS10
B	ALA98
B	GLY133
C	LYS10
C	ALA98
C	GLY133

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase => ECO:0000250

Chain	Residue	Details
A	GLY101
B	GLY101
C	GLY101
D	GLY101

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
A	LYS15
A	GLY12

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
B	LYS15
B	GLY12

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
C	LYS15
C	GLY12

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1f48

Chain	Residue	Details
D	LYS15
D	GLY12

site_id	MCSA1
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
A	GLY11	electrostatic stabiliser, hydrogen bond donor
A	SER16	electrostatic stabiliser, hydrogen bond donor
A	ALA42	electrostatic stabiliser, hydrogen bond donor
A	VAL130	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
B	GLY11	electrostatic stabiliser, hydrogen bond donor
B	SER16	electrostatic stabiliser, hydrogen bond donor
B	ALA42	electrostatic stabiliser, hydrogen bond donor
B	VAL130	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
C	GLY11	electrostatic stabiliser, hydrogen bond donor
C	SER16	electrostatic stabiliser, hydrogen bond donor
C	ALA42	electrostatic stabiliser, hydrogen bond donor
C	VAL130	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	4
Details	M-CSA 212

Chain	Residue	Details
D	GLY11	electrostatic stabiliser, hydrogen bond donor
D	SER16	electrostatic stabiliser, hydrogen bond donor
D	ALA42	electrostatic stabiliser, hydrogen bond donor
D	VAL130	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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