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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RJE

Aerococcus viridans L-lactate oxidase 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FNR A 401

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	PYR402
A	HOH501
A	HOH508
A	HOH514
A	ILE94
A	GLY95
A	SER122
A	GLN144
A	TYR146
A	THR172
A	LYS241

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PYR A 402

Chain	Residue
A	TYR40
A	TYR124
A	TYR146
A	ARG181
A	LEU211
A	TYR215
A	HIS265
A	ARG268
A	FNR401
A	HOH695

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 403

Chain	Residue
A	GLU26
A	LYS51
A	HOH510
A	HOH552

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FNR B 401

Chain	Residue
B	ALA92
B	PRO93
B	ILE94
B	GLY95
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	PYR402
B	HOH503
B	HOH511
B	HOH519
B	HOH693

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PYR B 402

Chain	Residue
B	TYR40
B	TYR146
B	ARG181
B	LEU211
B	TYR215
B	HIS265
B	ARG268
B	FNR401
B	HOH693

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 403

Chain	Residue
B	GLU26
B	LYS51
B	HOH510
B	HOH529

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FNR C 401

Chain	Residue
C	ALA92
C	PRO93
C	ILE94
C	GLY95
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	VAL299
C	ARG300
C	GLY319
C	ARG320
C	PYR402
C	HOH501
C	HOH511
C	HOH531

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PYR C 402

Chain	Residue
C	TYR40
C	TYR146
C	ARG181
C	LEU211
C	HIS265
C	ARG268
C	FNR401
C	HOH735

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 403

Chain	Residue
C	GLU26
C	LYS51
C	HOH518
C	HOH522

site_id	BC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FNR D 401

Chain	Residue
D	ALA92
D	PRO93
D	ILE94
D	GLY95
D	SER122
D	GLN144
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	PYR402
D	HOH502
D	HOH506
D	HOH541
D	HOH634

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PYR D 402

Chain	Residue
D	TYR40
D	TYR124
D	TYR146
D	ARG181
D	LEU211
D	TYR215
D	HIS265
D	ARG268
D	FNR401
D	HOH634

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	4
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:27302031

Chain	Residue	Details
A	HIS265
B	HIS265
C	HIS265
D	HIS265

site_id	SWS_FT_FI2
Number of Residues	24
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	TYR215
B	HIS265
B	ARG268
C	TYR40
C	TYR146
C	ARG181
C	TYR215
C	HIS265
C	ARG268
D	TYR40
A	TYR146
D	TYR146
D	ARG181
D	TYR215
D	HIS265
D	ARG268
A	ARG181
A	TYR215
A	HIS265
A	ARG268
B	TYR40
B	TYR146
B	ARG181

site_id	SWS_FT_FI3
Number of Residues	12
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
A	ASP296
A	ARG320
B	PRO93
B	ASP296
B	ARG320
C	PRO93
C	ASP296
C	ARG320

site_id	SWS_FT_FI4
Number of Residues	16
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
A	THR172
A	LYS241
A	SER263
B	SER122
B	THR172
B	LYS241
B	SER263
C	SER122

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:17517371, ECO:0007744\|PDB:2E77

Chain	Residue	Details
A	GLN144
B	GLN144
C	GLN144
D	GLN144

site_id	SWS_FT_FI6
Number of Residues	4
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	TYR215
B	TYR215
C	TYR215
D	TYR215

223532

PDB entries from 2024-08-07

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