2E77

Crystal structure of L-lactate oxidase with pyruvate complex

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 FMN A 4512

Chain	Residue
A	ILE41
A	LYS241
A	SER263
A	HIS265
A	GLY266
A	ARG268
A	ASP296
A	SER297
A	GLY298
A	ARG300
A	GLY319
A	ALA92
A	ARG320
A	PYR4442
A	HOH4529
A	HOH4530
A	HOH4550
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 4442

Chain	Residue
A	TYR40
A	ALA95
A	TYR124
A	TYR146
A	ARG181
A	TYR215
A	HIS265
A	ARG268
A	FMN4512

---

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN B 1512

Chain	Residue
B	ALA1092
B	PRO1093
B	ILE1094
B	ALA1095
B	SER1122
B	GLN1144
B	TYR1146
B	THR1172
B	LYS1241
B	SER1263
B	HIS1265
B	GLY1266
B	ARG1268
B	ASP1296
B	SER1297
B	GLY1298
B	ARG1300
B	GLY1319
B	ARG1320
B	PYR1442
B	HOH1515
B	HOH1527
B	HOH1566

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PYR B 1442

Chain	Residue
B	TYR1040
B	ALA1095
B	TYR1124
B	TYR1146
B	ARG1181
B	LEU1211
B	TYR1215
B	HIS1265
B	ARG1268
B	FMN1512

---

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN C 2512

Chain	Residue
C	ILE2041
C	ALA2092
C	PRO2093
C	ILE2094
C	ALA2095
C	SER2122
C	GLN2144
C	TYR2146
C	THR2172
C	LYS2241
C	SER2263
C	HIS2265
C	GLY2266
C	ARG2268
C	ASP2296
C	SER2297
C	GLY2298
C	ARG2300
C	GLY2319
C	ARG2320
C	HOH2525
C	HOH2527
C	HOH2555

---

site_id	AC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN D 3512

Chain	Residue
D	HIS3265
D	GLY3266
D	ARG3268
D	ASP3296
D	SER3297
D	GLY3298
D	ARG3300
D	GLY3319
D	ARG3320
D	PYR3442
D	HOH3534
D	HOH3540
D	HOH3542
D	ALA3092
D	PRO3093
D	ILE3094
D	ALA3095
D	SER3122
D	GLN3144
D	TYR3146
D	THR3172
D	LYS3241
D	SER3263

---

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PYR D 3442

Chain	Residue
D	TYR3040
D	ALA3095
D	TYR3124
D	TYR3146
D	ARG3181
D	TYR3215
D	HIS3265
D	ARG3268
D	FMN3512

---

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	HIS1265
C	HIS2265
D	HIS3265

---

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	TYR1215
B	HIS1265
B	ARG1268
C	TYR2040
C	TYR2146
C	ARG2181
C	TYR2215
C	HIS2265
C	ARG2268
D	TYR3040
A	TYR146
D	TYR3146
D	ARG3181
D	TYR3215
D	HIS3265
D	ARG3268
A	ARG181
A	TYR215
A	HIS265
A	ARG268
B	TYR1040
B	TYR1146
B	ARG1181

---

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	PRO3093
D	ASP3296
D	ARG3320
A	ASP296
A	ARG320
B	PRO1093
B	ASP1296
B	ARG1320
C	PRO2093
C	ASP2296
C	ARG2320

---

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	THR2172
C	LYS2241
C	SER2263
D	SER3122
D	THR3172
D	LYS3241
D	SER3263
A	THR172
A	LYS241
A	SER263
B	SER1122
B	THR1172
B	LYS1241
B	SER1263
C	SER2122

---

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	GLN1144
C	GLN2144
D	GLN3144

---

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	TYR1215
C	TYR2215
D	TYR3215

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
A	TYR40
A	ARG268
A	ASP174
A	HIS265
A	TYR146

---

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
B	ASP1174
B	HIS1265
B	TYR1146
B	TYR1040
B	ARG1268

---

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
C	HIS2265
C	ARG2268
C	ASP2174
C	TYR2040
C	TYR2146

---

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
D	ARG3268
D	TYR3146
D	ASP3174
D	TYR3040
D	HIS3265

---

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
A	ARG268
A	HIS265
A	ASP174
A	TYR146

---

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
B	ASP1174
B	HIS1265
B	TYR1146
B	ARG1268

---

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
C	HIS2265
C	ARG2268
C	ASP2174
C	TYR2146

---

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1fcb

Chain	Residue	Details
D	ARG3268
D	TYR3146
D	ASP3174
D	HIS3265

---