Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OHH

Crystal Structure of coenzyme F420H2 oxidase (FprA), a diiron flavoprotein, active oxidized 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
A	0052765	molecular_function	coenzyme F420H2 oxidase activity
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
B	0052765	molecular_function	coenzyme F420H2 oxidase activity
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
D	0052765	molecular_function	coenzyme F420H2 oxidase activity
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
E	0052765	molecular_function	coenzyme F420H2 oxidase activity

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	FE502

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 502

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

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 1501

Chain	Residue
B	ASP87
B	HIS88
B	ASP170
B	HIS233
B	FE1502

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 1502

Chain	Residue
B	HIS83
B	GLU85
B	HIS151
B	ASP170
B	FE1501

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE D 2501

Chain	Residue
D	ASP87
D	HIS88
D	ASP170
D	HIS233
D	SO42414
D	FE2502

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE D 2502

Chain	Residue
D	HIS83
D	GLU85
D	HIS151
D	ASP170
D	SO42414
D	FE2501

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE E 3501

Chain	Residue
E	ASP87
E	HIS88
E	ASP170
E	HIS233
E	FE3502
E	HOH3971

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE E 3502

Chain	Residue
E	HIS83
E	GLU85
E	HIS151
E	ASP170
E	FE3501
E	HOH3971

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 D 2414

Chain	Residue
D	TYR25
D	HIS26
D	GLU85
D	ASP87
D	HIS151
D	ASP170
D	HIS175
D	LEU202
D	HIS233
D	FE2501
D	FE2502

site_id	BC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FMN A 701

Chain	Residue
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
A	GLY356
A	TYR381
A	HOH736
A	HOH887
B	HIS26
B	HIS151
B	TRP152
B	LEU202
B	HOH1716

site_id	BC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FMN B 1701

Chain	Residue
B	ASN355
B	GLY356
B	TYR381
B	HOH1728
B	HOH1731
A	GLU85
A	HIS151
A	TRP152
A	LEU202
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

site_id	BC3
Number of Residues	24
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	HOH2705
D	HOH2793
E	GLU85
E	HIS151
E	TRP152
E	LEU202

site_id	BC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FMN E 3701

Chain	Residue
D	GLU85
D	HIS151
D	TRP152
D	LEU202
D	HOH2886
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
E	TYR381
E	HOH3730
E	HOH3813

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	12
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
A	GLU85
A	ASP87
B	HIS83
B	GLU85
B	ASP87
D	HIS83
D	GLU85
D	ASP87

site_id	SWS_FT_FI2
Number of Residues	24
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
A	HIS233
A	THR265
A	THR317
A	SER351
B	HIS88
B	ASP170
B	HIS233

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:17480207, ECO:0007744\|PDB:2OHH

Chain	Residue	Details
A	HIS151
B	HIS151
D	HIS151
E	HIS151

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP87

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

Chain	Residue	Details
B	ASP87

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

Chain	Residue	Details
D	ASP87

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

Chain	Residue	Details
E	ASP87

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 2bmi

Chain	Residue	Details
A	ASN201
A	ASP87

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 2bmi

Chain	Residue	Details
B	ASN201
B	ASP87

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 2bmi

Chain	Residue	Details
D	ASN201
D	ASP87

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 2bmi

Chain	Residue	Details
E	ASN201
E	ASP87

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