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5EBU

Aerococcus viridans L-lactate oxidase Y215F mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0010181molecular_functionFMN binding
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0010181molecular_functionFMN binding
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0010181molecular_functionFMN binding
E0016491molecular_functionoxidoreductase activity
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0010181molecular_functionFMN binding
F0016491molecular_functionoxidoreductase activity
F0046872molecular_functionmetal ion binding
G0000166molecular_functionnucleotide binding
G0010181molecular_functionFMN binding
G0016491molecular_functionoxidoreductase activity
G0046872molecular_functionmetal ion binding
H0000166molecular_functionnucleotide binding
H0010181molecular_functionFMN binding
H0016491molecular_functionoxidoreductase activity
H0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue FMN A 400
ChainResidue
AALA92
ASER263
AHIS265
AGLY266
AARG268
AASP296
ASER297
AGLY298
AVAL299
AARG300
AGLY319
APRO93
AARG320
APYR401
AHOH520
AHOH523
AILE94
AALA95
ASER122
AGLN144
ATYR146
ATHR172
ALYS241

site_idAC2
Number of Residues9
Detailsbinding site for residue PYR A 401
ChainResidue
ATYR40
ATYR124
ATYR146
AARG181
ALEU211
APHE215
AHIS265
AARG268
AFMN400

site_idAC3
Number of Residues22
Detailsbinding site for residue FMN B 400
ChainResidue
BPRO93
BILE94
BALA95
BSER122
BGLN144
BTYR146
BTHR172
BLYS241
BSER263
BHIS265
BGLY266
BARG268
BASP296
BSER297
BGLY298
BARG300
BGLY319
BARG320
BPYR401
BHOH510
BHOH512
BHOH532

site_idAC4
Number of Residues8
Detailsbinding site for residue PYR B 401
ChainResidue
BTYR40
BTYR124
BTYR146
BARG181
BLEU211
BHIS265
BARG268
BFMN400

site_idAC5
Number of Residues22
Detailsbinding site for residue FMN C 400
ChainResidue
CILE41
CALA92
CPRO93
CILE94
CALA95
CSER122
CGLN144
CTYR146
CTHR172
CLYS241
CSER263
CHIS265
CGLY266
CARG268
CASP296
CSER297
CGLY298
CARG300
CGLY319
CARG320
CPYR401
CHOH505

site_idAC6
Number of Residues7
Detailsbinding site for residue PYR C 401
ChainResidue
CTYR40
CTYR124
CTYR146
CARG181
CHIS265
CARG268
CFMN400

site_idAC7
Number of Residues25
Detailsbinding site for residue FMN D 400
ChainResidue
DTYR146
DTHR172
DLYS241
DSER263
DHIS265
DGLY266
DARG268
DASP296
DSER297
DGLY298
DVAL299
DARG300
DGLY319
DARG320
DPYR401
DHOH502
DHOH512
DTYR40
DILE41
DALA92
DPRO93
DILE94
DALA95
DSER122
DGLN144

site_idAC8
Number of Residues6
Detailsbinding site for residue PYR D 401
ChainResidue
DTYR40
DTYR146
DARG181
DHIS265
DARG268
DFMN400

site_idAC9
Number of Residues24
Detailsbinding site for residue FMN E 400
ChainResidue
EILE41
EALA92
EPRO93
EILE94
EALA95
ESER122
EGLN144
ETYR146
ETHR172
ELYS241
ESER263
EHIS265
EGLY266
EARG268
EASP296
ESER297
EGLY298
EVAL299
EARG300
EGLY319
EARG320
EPYR401
EHOH501
EHOH511

site_idAD1
Number of Residues7
Detailsbinding site for residue PYR E 401
ChainResidue
ETYR40
ETYR146
EARG181
ELEU211
EHIS265
EARG268
EFMN400

site_idAD2
Number of Residues22
Detailsbinding site for residue FMN F 400
ChainResidue
FILE41
FPRO93
FILE94
FALA95
FSER122
FGLN144
FTYR146
FTHR172
FLYS241
FSER263
FHIS265
FGLY266
FARG268
FASP296
FSER297
FGLY298
FARG300
FGLY319
FARG320
FPYR401
FHOH504
FHOH531

site_idAD3
Number of Residues8
Detailsbinding site for residue PYR F 401
ChainResidue
FTYR40
FTYR124
FTYR146
FARG181
FLEU211
FHIS265
FARG268
FFMN400

site_idAD4
Number of Residues22
Detailsbinding site for residue FMN G 400
ChainResidue
GILE41
GPRO93
GILE94
GALA95
GSER122
GGLN144
GTYR146
GTHR172
GLYS241
GSER263
GHIS265
GGLY266
GARG268
GASP296
GSER297
GGLY298
GARG300
GGLY319
GARG320
GPYR401
GHOH515
GHOH525

site_idAD5
Number of Residues8
Detailsbinding site for residue PYR G 401
ChainResidue
GTYR40
GALA95
GTYR124
GTYR146
GARG181
GHIS265
GARG268
GFMN400

site_idAD6
Number of Residues24
Detailsbinding site for residue FMN H 400
ChainResidue
HILE41
HALA92
HPRO93
HILE94
HALA95
HSER122
HGLN144
HTYR146
HTHR172
HLYS241
HSER263
HHIS265
HGLY266
HARG268
HASP296
HSER297
HGLY298
HVAL299
HARG300
HGLY319
HARG320
HPYR401
HHOH517
HHOH519

site_idAD7
Number of Residues6
Detailsbinding site for residue PYR H 401
ChainResidue
HTYR40
HTYR146
HARG181
HHIS265
HARG268
HFMN400

Functional Information from PROSITE/UniProt
site_idPS00557
Number of Residues7
DetailsFMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGARQ
ChainResidueDetails
ASER263-GLN269

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2136
DetailsDomain: {"description":"FMN hydroxy acid dehydrogenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"27302031","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues46
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues56
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues32
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17517371","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E77","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsSite: {"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"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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