Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OHI

Crystal Structure of coenzyme F420H2 oxidase (FprA), a diiron flavoprotein, reduced state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009055	molecular_function	electron transfer activity
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
B	0009055	molecular_function	electron transfer activity
B	0010181	molecular_function	FMN binding
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
D	0009055	molecular_function	electron transfer activity
D	0010181	molecular_function	FMN binding
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
E	0009055	molecular_function	electron transfer activity
E	0010181	molecular_function	FMN binding
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
G	0009055	molecular_function	electron transfer activity
G	0010181	molecular_function	FMN binding
G	0016491	molecular_function	oxidoreductase activity
G	0046872	molecular_function	metal ion binding
H	0009055	molecular_function	electron transfer activity
H	0010181	molecular_function	FMN binding
H	0016491	molecular_function	oxidoreductase activity
H	0046872	molecular_function	metal ion binding
I	0009055	molecular_function	electron transfer activity
I	0010181	molecular_function	FMN binding
I	0016491	molecular_function	oxidoreductase activity
I	0046872	molecular_function	metal ion binding
J	0009055	molecular_function	electron transfer activity
J	0010181	molecular_function	FMN binding
J	0016491	molecular_function	oxidoreductase activity
J	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 501

Chain	Residue
A	ASP87
A	HIS88
A	ASP170
A	HIS233
A	FE503

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 1501

Chain	Residue
B	HOH1739
B	ASP87
B	HIS88
B	ASP170
B	HIS233

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE D 2501

Chain	Residue
D	ASP87
D	HIS88
D	ASP170
D	HIS233
D	HOH2743

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE E 3501

Chain	Residue
E	ASP87
E	HIS88
E	ASP170
E	HIS233

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE G 501

Chain	Residue
G	ASP87
G	HIS88
G	ASP170
G	HIS233
G	FE503

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE H 1501

Chain	Residue
H	GLU85
H	ASP87
H	HIS88
H	ASP170
H	HIS233
H	FE1503

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE I 2501

Chain	Residue
I	ASP87
I	HIS88
I	ASP170
I	HIS233

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE J 3501

Chain	Residue
J	ASP87
J	HIS88
J	ASP170
J	HIS233
J	FE3503

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 503

Chain	Residue
A	HIS83
A	GLU85
A	HIS151
A	ASP170
A	FE501

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE B 1503

Chain	Residue
B	HIS83
B	GLU85
B	HIS151
B	ASP170

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE D 2503

Chain	Residue
D	HIS83
D	GLU85
D	HIS151
D	ASP170

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE E 3503

Chain	Residue
E	HIS83
E	GLU85
E	HIS151
E	ASP170

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE G 503

Chain	Residue
G	HIS83
G	GLU85
G	HIS151
G	ASP170
G	FE501

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE H 1503

Chain	Residue
H	HIS83
H	GLU85
H	HIS151
H	ASP170
H	FE1501

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE I 2503

Chain	Residue
I	HIS83
I	GLU85
I	HIS151
I	ASP170

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE J 3503

Chain	Residue
J	HIS83
J	GLU85
J	HIS151
J	ASP170
J	FE3501

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL J 3504

Chain	Residue
J	LYS337
J	ASN339
J	ARG340

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL J 3505

Chain	Residue
H	MET282
J	PRO179
J	ARG181

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL D 2504

Chain	Residue
D	ARG340

site_id	CC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL H 1504

Chain	Residue
H	GLU368

site_id	CC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN A 701

Chain	Residue
A	GLY356
A	TYR381
A	HOH709
A	HOH732
B	GLU85
B	TRP152
A	THR265
A	MET266
A	HIS267
A	GLY268
A	SER269
A	THR270
A	PRO316
A	THR317
A	ILE318
A	TYR319
A	ASP320
A	SER351
A	MET352
A	GLY353
A	GLY354
A	ASN355

site_id	CC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN B 1701

Chain	Residue
A	HIS151
A	TRP152
B	THR265
B	MET266
B	HIS267
B	GLY268
B	SER269
B	THR270
B	PRO316
B	THR317
B	ILE318
B	TYR319
B	ASP320
B	SER351
B	MET352
B	GLY353
B	GLY354
B	ASN355
B	GLY356
B	TYR381
B	HOH1717
B	HOH1723

site_id	CC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE FMN D 2701

Chain	Residue
D	THR265
D	MET266
D	HIS267
D	GLY268
D	SER269
D	THR270
D	PRO316
D	THR317
D	ILE318
D	TYR319
D	ASP320
D	SER351
D	MET352
D	GLY353
D	GLY354
D	ASN355
D	GLY356
D	TYR381
D	HOH2735
E	GLU85
E	TRP152

site_id	CC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FMN E 3701

Chain	Residue
D	TRP152
E	THR265
E	MET266
E	HIS267
E	GLY268
E	SER269
E	THR270
E	PRO316
E	THR317
E	ILE318
E	TYR319
E	ASP320
E	SER351
E	MET352
E	GLY353
E	GLY354
E	ASN355
E	GLY356

site_id	CC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN G 702

Chain	Residue
G	THR265
G	MET266
G	HIS267
G	GLY268
G	SER269
G	THR270
G	PRO316
G	THR317
G	ILE318
G	TYR319
G	ASP320
G	SER351
G	MET352
G	GLY353
G	GLY354
G	ASN355
G	GLY356
G	TYR381
G	HOH704
G	HOH708
H	GLU85
H	HIS151
H	TRP152

site_id	CC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FMN H 1702

Chain	Residue
G	GLU85
G	HIS151
G	TRP152
H	THR265
H	MET266
H	HIS267
H	GLY268
H	SER269
H	THR270
H	PRO316
H	THR317
H	ILE318
H	TYR319
H	ASP320
H	SER351
H	MET352
H	GLY353
H	GLY354
H	ASN355
H	GLY356
H	TYR381
H	HOH1715

site_id	CC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE FMN I 2702

Chain	Residue
I	THR265
I	MET266
I	HIS267
I	GLY268
I	SER269
I	THR270
I	PRO316
I	THR317
I	ILE318
I	TYR319
I	ASP320
I	SER351
I	MET352
I	GLY353
I	GLY354
I	ASN355
I	GLY356
I	TYR381
I	HOH2714
J	HIS151
J	TRP152

site_id	DC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE FMN J 3702

Chain	Residue
I	HIS151
I	TRP152
I	LEU202
J	THR265
J	MET266
J	HIS267
J	GLY268
J	SER269
J	THR270
J	PRO316
J	THR317
J	ILE318
J	TYR319
J	ASP320
J	SER351
J	MET352
J	GLY353
J	GLY354
J	ASN355
J	GLY356
J	TYR381

Functional Information from PROSITE/UniProt

site_id	PS00201
Number of Residues	17
Details	FLAVODOXIN Flavodoxin signature. VIYdTMhGsTRkmAHaI

Chain	Residue	Details
A	VAL261-ILE277

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:17480207, ECO:0007744\|PDB:2OHH, ECO:0007744\|PDB:2OHI

Chain	Residue	Details
A	HIS83
E	HIS83
E	GLU85
E	ASP87
G	HIS83
G	GLU85
G	ASP87
H	HIS83
H	GLU85
H	ASP87
I	HIS83
A	GLU85
I	GLU85
I	ASP87
J	HIS83
J	GLU85
J	ASP87
A	ASP87
B	HIS83
B	GLU85
B	ASP87
D	HIS83
D	GLU85
D	ASP87

site_id	SWS_FT_FI2
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:17480207, ECO:0007744\|PDB:2OHH, ECO:0007744\|PDB:2OHI, ECO:0007744\|PDB:2OHJ

Chain	Residue	Details
A	HIS88
B	THR265
B	THR317
B	SER351
D	HIS88
D	ASP170
D	HIS233
D	THR265
D	THR317
D	SER351
E	HIS88
A	ASP170
E	ASP170
E	HIS233
E	THR265
E	THR317
E	SER351
G	HIS88
G	ASP170
G	HIS233
G	THR265
G	THR317
A	HIS233
G	SER351
H	HIS88
H	ASP170
H	HIS233
H	THR265
H	THR317
H	SER351
I	HIS88
I	ASP170
I	HIS233
A	THR265
I	THR265
I	THR317
I	SER351
J	HIS88
J	ASP170
J	HIS233
J	THR265
J	THR317
J	SER351
A	THR317
A	SER351
B	HIS88
B	ASP170
B	HIS233

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:17480207, ECO:0007744\|PDB:2OHH

Chain	Residue	Details
A	HIS151
B	HIS151
D	HIS151
E	HIS151
G	HIS151
H	HIS151
I	HIS151
J	HIS151

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