Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5EBU

Aerococcus viridans L-lactate oxidase Y215F mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0010181	molecular_function	FMN binding
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0010181	molecular_function	FMN binding
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0010181	molecular_function	FMN binding
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0010181	molecular_function	FMN binding
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
F	0000166	molecular_function	nucleotide binding
F	0010181	molecular_function	FMN binding
F	0016491	molecular_function	oxidoreductase activity
F	0046872	molecular_function	metal ion binding
G	0000166	molecular_function	nucleotide binding
G	0010181	molecular_function	FMN binding
G	0016491	molecular_function	oxidoreductase activity
G	0046872	molecular_function	metal ion binding
H	0000166	molecular_function	nucleotide binding
H	0010181	molecular_function	FMN binding
H	0016491	molecular_function	oxidoreductase activity
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue FMN A 400

Chain	Residue
A	ALA92
A	SER263
A	HIS265
A	GLY266
A	ARG268
A	ASP296
A	SER297
A	GLY298
A	VAL299
A	ARG300
A	GLY319
A	PRO93
A	ARG320
A	PYR401
A	HOH520
A	HOH523
A	ILE94
A	ALA95
A	SER122
A	GLN144
A	TYR146
A	THR172
A	LYS241

site_id	AC2
Number of Residues	9
Details	binding site for residue PYR A 401

Chain	Residue
A	TYR40
A	TYR124
A	TYR146
A	ARG181
A	LEU211
A	PHE215
A	HIS265
A	ARG268
A	FMN400

site_id	AC3
Number of Residues	22
Details	binding site for residue FMN B 400

Chain	Residue
B	PRO93
B	ILE94
B	ALA95
B	SER122
B	GLN144
B	TYR146
B	THR172
B	LYS241
B	SER263
B	HIS265
B	GLY266
B	ARG268
B	ASP296
B	SER297
B	GLY298
B	ARG300
B	GLY319
B	ARG320
B	PYR401
B	HOH510
B	HOH512
B	HOH532

site_id	AC4
Number of Residues	8
Details	binding site for residue PYR B 401

Chain	Residue
B	TYR40
B	TYR124
B	TYR146
B	ARG181
B	LEU211
B	HIS265
B	ARG268
B	FMN400

site_id	AC5
Number of Residues	22
Details	binding site for residue FMN C 400

Chain	Residue
C	ILE41
C	ALA92
C	PRO93
C	ILE94
C	ALA95
C	SER122
C	GLN144
C	TYR146
C	THR172
C	LYS241
C	SER263
C	HIS265
C	GLY266
C	ARG268
C	ASP296
C	SER297
C	GLY298
C	ARG300
C	GLY319
C	ARG320
C	PYR401
C	HOH505

site_id	AC6
Number of Residues	7
Details	binding site for residue PYR C 401

Chain	Residue
C	TYR40
C	TYR124
C	TYR146
C	ARG181
C	HIS265
C	ARG268
C	FMN400

site_id	AC7
Number of Residues	25
Details	binding site for residue FMN D 400

Chain	Residue
D	TYR146
D	THR172
D	LYS241
D	SER263
D	HIS265
D	GLY266
D	ARG268
D	ASP296
D	SER297
D	GLY298
D	VAL299
D	ARG300
D	GLY319
D	ARG320
D	PYR401
D	HOH502
D	HOH512
D	TYR40
D	ILE41
D	ALA92
D	PRO93
D	ILE94
D	ALA95
D	SER122
D	GLN144

site_id	AC8
Number of Residues	6
Details	binding site for residue PYR D 401

Chain	Residue
D	TYR40
D	TYR146
D	ARG181
D	HIS265
D	ARG268
D	FMN400

site_id	AC9
Number of Residues	24
Details	binding site for residue FMN E 400

Chain	Residue
E	ILE41
E	ALA92
E	PRO93
E	ILE94
E	ALA95
E	SER122
E	GLN144
E	TYR146
E	THR172
E	LYS241
E	SER263
E	HIS265
E	GLY266
E	ARG268
E	ASP296
E	SER297
E	GLY298
E	VAL299
E	ARG300
E	GLY319
E	ARG320
E	PYR401
E	HOH501
E	HOH511

site_id	AD1
Number of Residues	7
Details	binding site for residue PYR E 401

Chain	Residue
E	TYR40
E	TYR146
E	ARG181
E	LEU211
E	HIS265
E	ARG268
E	FMN400

site_id	AD2
Number of Residues	22
Details	binding site for residue FMN F 400

Chain	Residue
F	ILE41
F	PRO93
F	ILE94
F	ALA95
F	SER122
F	GLN144
F	TYR146
F	THR172
F	LYS241
F	SER263
F	HIS265
F	GLY266
F	ARG268
F	ASP296
F	SER297
F	GLY298
F	ARG300
F	GLY319
F	ARG320
F	PYR401
F	HOH504
F	HOH531

site_id	AD3
Number of Residues	8
Details	binding site for residue PYR F 401

Chain	Residue
F	TYR40
F	TYR124
F	TYR146
F	ARG181
F	LEU211
F	HIS265
F	ARG268
F	FMN400

site_id	AD4
Number of Residues	22
Details	binding site for residue FMN G 400

Chain	Residue
G	ILE41
G	PRO93
G	ILE94
G	ALA95
G	SER122
G	GLN144
G	TYR146
G	THR172
G	LYS241
G	SER263
G	HIS265
G	GLY266
G	ARG268
G	ASP296
G	SER297
G	GLY298
G	ARG300
G	GLY319
G	ARG320
G	PYR401
G	HOH515
G	HOH525

site_id	AD5
Number of Residues	8
Details	binding site for residue PYR G 401

Chain	Residue
G	TYR40
G	ALA95
G	TYR124
G	TYR146
G	ARG181
G	HIS265
G	ARG268
G	FMN400

site_id	AD6
Number of Residues	24
Details	binding site for residue FMN H 400

Chain	Residue
H	ILE41
H	ALA92
H	PRO93
H	ILE94
H	ALA95
H	SER122
H	GLN144
H	TYR146
H	THR172
H	LYS241
H	SER263
H	HIS265
H	GLY266
H	ARG268
H	ASP296
H	SER297
H	GLY298
H	VAL299
H	ARG300
H	GLY319
H	ARG320
H	PYR401
H	HOH517
H	HOH519

site_id	AD7
Number of Residues	6
Details	binding site for residue PYR H 401

Chain	Residue
H	TYR40
H	TYR146
H	ARG181
H	HIS265
H	ARG268
H	FMN400

Functional Information from PROSITE/UniProt

site_id	PS00557
Number of Residues	7
Details	FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGARQ

Chain	Residue	Details
A	SER263-GLN269

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:27302031

Chain	Residue	Details
A	HIS265
B	HIS265
C	HIS265
D	HIS265
E	HIS265
F	HIS265
G	HIS265
H	HIS265

site_id	SWS_FT_FI2
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:17517371, ECO:0000269\|PubMed:25423902, ECO:0007744\|PDB:2E77, ECO:0007744\|PDB:4RJE

Chain	Residue	Details
A	TYR40
B	PHE215
B	HIS265
B	ARG268
C	TYR40
C	TYR146
C	ARG181
C	PHE215
C	HIS265
C	ARG268
D	TYR40
A	TYR146
D	TYR146
D	ARG181
D	PHE215
D	HIS265
D	ARG268
E	TYR40
E	TYR146
E	ARG181
E	PHE215
E	HIS265
A	ARG181
E	ARG268
F	TYR40
F	TYR146
F	ARG181
F	PHE215
F	HIS265
F	ARG268
G	TYR40
G	TYR146
G	ARG181
A	PHE215
G	PHE215
G	HIS265
G	ARG268
H	TYR40
H	TYR146
H	ARG181
H	PHE215
H	HIS265
H	ARG268
A	HIS265
A	ARG268
B	TYR40
B	TYR146
B	ARG181

site_id	SWS_FT_FI3
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:17517371, ECO:0000269\|PubMed:18367206, ECO:0007744\|PDB:2DU2, ECO:0007744\|PDB:2E77, ECO:0007744\|PDB:2NLI

Chain	Residue	Details
A	PRO93
D	PRO93
D	ASP296
D	ARG320
E	PRO93
E	ASP296
E	ARG320
F	PRO93
F	ASP296
F	ARG320
G	PRO93
A	ASP296
G	ASP296
G	ARG320
H	PRO93
H	ASP296
H	ARG320
A	ARG320
B	PRO93
B	ASP296
B	ARG320
C	PRO93
C	ASP296
C	ARG320

site_id	SWS_FT_FI4
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269\|PubMed:17517371, ECO:0000269\|PubMed:18367206, ECO:0007744\|PDB:2E77, ECO:0007744\|PDB:2NLI

Chain	Residue	Details
A	SER122
C	THR172
C	LYS241
C	SER263
D	SER122
D	THR172
D	LYS241
D	SER263
E	SER122
E	THR172
E	LYS241
A	THR172
E	SER263
F	SER122
F	THR172
F	LYS241
F	SER263
G	SER122
G	THR172
G	LYS241
G	SER263
H	SER122
A	LYS241
H	THR172
H	LYS241
H	SER263
A	SER263
B	SER122
B	THR172
B	LYS241
B	SER263
C	SER122

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:17517371, ECO:0007744\|PDB:2E77

Chain	Residue	Details
A	GLN144
B	GLN144
C	GLN144
D	GLN144
E	GLN144
F	GLN144
G	GLN144
H	GLN144

site_id	SWS_FT_FI6
Number of Residues	8
Details	SITE: Is suggested to participate in control of opening/closing motions of the active-site lid in A.viridans LOX => ECO:0000305\|PubMed:27302031

Chain	Residue	Details
A	PHE215
B	PHE215
C	PHE215
D	PHE215
E	PHE215
F	PHE215
G	PHE215
H	PHE215

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