4YL2

Aerococcus viridans L-lactate oxidase Y191F 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	25
Details	binding site for residue FMN A 401

Chain	Residue
A	ILE41
A	LYS241
A	SER263
A	HIS265
A	GLY266
A	ARG268
A	ASP296
A	SER297
A	GLY298
A	VAL299
A	ARG300
A	ALA92
A	GLY319
A	ARG320
A	PYR402
A	HOH517
A	HOH519
A	HOH579
A	PRO93
A	ILE94
A	ALA95
A	SER122
A	GLN144
A	TYR146
A	THR172

---

site_id	AC2
Number of Residues	9
Details	binding site for residue PYR A 402

Chain	Residue
A	TYR40
A	ALA95
A	TYR124
A	TYR146
A	ARG181
A	TYR215
A	HIS265
A	ARG268
A	FMN401

---

site_id	AC3
Number of Residues	24
Details	binding site for residue FMN B 401

Chain	Residue
B	ILE41
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	VAL299
B	ARG300
B	GLY319
B	ARG320
B	PYR402
B	HOH529
B	HOH538
B	HOH549

---

site_id	AC4
Number of Residues	10
Details	binding site for residue PYR B 402

Chain	Residue
B	TYR40
B	ALA95
B	TYR124
B	TYR146
B	ARG181
B	LEU211
B	TYR215
B	HIS265
B	ARG268
B	FMN401

---

site_id	AC5
Number of Residues	25
Details	binding site for residue FMN C 401

Chain	Residue
C	TYR40
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	PYR402
C	HOH555
C	HOH585
C	HOH625

---

site_id	AC6
Number of Residues	10
Details	binding site for residue PYR C 402

Chain	Residue
C	TYR215
C	HIS265
C	ARG268
C	FMN401
C	TYR40
C	ALA95
C	TYR124
C	TYR146
C	ARG181
C	LEU211

---

site_id	AC7
Number of Residues	25
Details	binding site for residue FMN D 401

Chain	Residue
D	TYR40
D	ILE41
D	ALA92
D	PRO93
D	ILE94
D	ALA95
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	ARG300
D	GLY319
D	ARG320
D	PYR402
D	HOH519
D	HOH526
D	HOH532

---

site_id	AC8
Number of Residues	9
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	FMN401

---

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	1068
Details	Domain: {"description":"FMN hydroxy acid dehydrogenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"27302031","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17517371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25423902","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RJE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17517371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18367206","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DU2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2E77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NLI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17517371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18367206","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E77","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NLI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17517371","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E77","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Site: {"description":"Is suggested to participate in control of opening/closing motions of the active-site lid in A.viridans LOX","evidences":[{"source":"PubMed","id":"27302031","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---