Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6Q93

MgADP-bound Fe protein of Vanadium nitrogenase 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	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 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	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 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	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051539	molecular_function	4 iron, 4 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	0046872	molecular_function	metal ion binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 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	8
Details	binding site for residue SF4 A 1001

Chain	Residue
A	CYS98
A	CYS133
A	GLY134
A	PHE136
B	CYS98
B	ALA99
B	CYS133
B	GLY134

site_id	AC2
Number of Residues	21
Details	binding site for residue ADP A 1002

Chain	Residue
A	ILE14
A	GLY15
A	LYS16
A	SER17
A	THR18
A	ASN186
A	VAL212
A	PRO213
A	ARG214
A	ASP215
A	VAL218
A	GLN219
A	GLU222
A	GLN237
A	TYR241
A	MG1003
A	HOH1104
A	HOH1120
A	HOH1135
A	HOH1136
A	GLY13

site_id	AC3
Number of Residues	6
Details	binding site for residue MG A 1003

Chain	Residue
A	SER17
A	ADP1002
A	HOH1104
A	HOH1120
A	HOH1121
A	HOH1135

site_id	AC4
Number of Residues	19
Details	binding site for residue ADP B 301

Chain	Residue
B	GLY13
B	ILE14
B	GLY15
B	LYS16
B	SER17
B	THR18
B	ASN186
B	VAL212
B	PRO213
B	ARG214
B	ASP215
B	VAL218
B	GLN219
B	GLU222
B	GLN237
B	MG302
B	HOH402
B	HOH405
B	HOH406

site_id	AC5
Number of Residues	6
Details	binding site for residue MG B 302

Chain	Residue
B	SER17
B	ASP40
B	ADP301
B	HOH402
B	HOH405
B	HOH406

site_id	AC6
Number of Residues	7
Details	binding site for residue SF4 C 1001

Chain	Residue
C	CYS98
C	ALA99
C	CYS133
C	GLY134
D	CYS98
D	CYS133
D	GLY134

site_id	AC7
Number of Residues	21
Details	binding site for residue ADP C 1002

Chain	Residue
C	GLY13
C	ILE14
C	GLY15
C	LYS16
C	SER17
C	THR18
C	ASN186
C	VAL212
C	PRO213
C	ARG214
C	ASP215
C	VAL218
C	GLN219
C	GLU222
C	GLN237
C	TYR241
C	MG1003
C	HOH1102
C	HOH1103
C	HOH1115
C	HOH1118

site_id	AC8
Number of Residues	7
Details	binding site for residue MG C 1003

Chain	Residue
C	SER17
C	ASP40
C	ADP1002
C	HOH1102
C	HOH1103
C	HOH1118
C	HOH1121

site_id	AC9
Number of Residues	3
Details	binding site for residue MG C 1004

Chain	Residue
C	GLU69
C	LEU71
C	GLU113

site_id	AD1
Number of Residues	22
Details	binding site for residue ADP D 301

Chain	Residue
D	GLY13
D	ILE14
D	GLY15
D	LYS16
D	SER17
D	THR18
D	ASN186
D	VAL212
D	PRO213
D	ARG214
D	ASP215
D	VAL218
D	GLN219
D	GLU222
D	GLN237
D	TYR241
D	MG302
D	HOH403
D	HOH408
D	HOH409
D	HOH411
C	MET157

site_id	AD2
Number of Residues	6
Details	binding site for residue MG D 302

Chain	Residue
D	SER17
D	ADP301
D	HOH403
D	HOH406
D	HOH408
D	HOH409

site_id	AD3
Number of Residues	8
Details	binding site for residue SF4 E 1001

Chain	Residue
E	CYS98
E	ALA99
E	CYS133
E	GLY134
F	CYS98
F	CYS133
F	GLY134
F	PHE136

site_id	AD4
Number of Residues	19
Details	binding site for residue ADP E 1002

Chain	Residue
E	GLY13
E	ILE14
E	GLY15
E	LYS16
E	SER17
E	THR18
E	ASN186
E	VAL212
E	PRO213
E	ARG214
E	ASP215
E	VAL218
E	GLN219
E	GLU222
E	GLN237
E	TYR241
E	MG1003
E	HOH1101
E	HOH1108

site_id	AD5
Number of Residues	6
Details	binding site for residue MG E 1003

Chain	Residue
E	SER17
E	ASP40
E	ADP1002
E	HOH1101
E	HOH1105
E	HOH1108

site_id	AD6
Number of Residues	21
Details	binding site for residue ADP F 301

Chain	Residue
F	GLY13
F	ILE14
F	GLY15
F	LYS16
F	SER17
F	THR18
F	ASN186
F	VAL212
F	PRO213
F	ARG214
F	ASP215
F	VAL218
F	GLN219
F	GLU222
F	GLN237
F	TYR241
F	MG302
F	HOH402
F	HOH407
F	HOH423
F	HOH438

site_id	AD7
Number of Residues	7
Details	binding site for residue MG F 302

Chain	Residue
F	SER17
F	ASP40
F	ADP301
F	HOH402
F	HOH407
F	HOH420
F	HOH423

site_id	AD8
Number of Residues	2
Details	binding site for residue MG F 303

Chain	Residue
F	GLU69
F	GLU113

site_id	AD9
Number of Residues	6
Details	binding site for residue SF4 G 1001

Chain	Residue
G	CYS98
G	CYS133
G	GLY134
H	CYS98
H	CYS133
H	GLY134

site_id	AE1
Number of Residues	22
Details	binding site for residue ADP G 1002

Chain	Residue
G	GLY13
G	ILE14
G	GLY15
G	LYS16
G	SER17
G	THR18
G	ASN186
G	VAL212
G	PRO213
G	ARG214
G	ASP215
G	VAL218
G	GLN219
G	GLU222
G	GLN237
G	TYR241
G	MG1003
G	HOH1111
G	HOH1117
G	HOH1118
G	HOH1119
H	MET157

site_id	AE2
Number of Residues	7
Details	binding site for residue MG G 1003

Chain	Residue
G	SER17
G	ASP40
G	ADP1002
G	HOH1111
G	HOH1114
G	HOH1117
G	HOH1119

site_id	AE3
Number of Residues	23
Details	binding site for residue ADP H 301

Chain	Residue
H	GLY13
H	ILE14
H	GLY15
H	LYS16
H	SER17
H	THR18
H	ASN186
H	VAL212
H	PRO213
H	ARG214
H	ASP215
H	VAL218
H	GLN219
H	GLU222
H	GLN237
H	TYR241
H	MG302
H	HOH403
H	HOH411
H	HOH413
H	HOH416
H	HOH422
H	HOH433

site_id	AE4
Number of Residues	7
Details	binding site for residue MG H 302

Chain	Residue
H	SER17
H	ASP40
H	ADP301
H	HOH403
H	HOH406
H	HOH416
H	HOH422

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	ASP126-PRO139

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

Chain	Residue	Details
A	GLU88-GLY100

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