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4RJE

Aerococcus viridans L-lactate oxidase 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
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FNR A 401
ChainResidue
AALA92
ASER263
AHIS265
AGLY266
AARG268
AASP296
ASER297
AGLY298
AVAL299
AARG300
AGLY319
APRO93
AARG320
APYR402
AHOH501
AHOH508
AHOH514
AILE94
AGLY95
ASER122
AGLN144
ATYR146
ATHR172
ALYS241

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYR A 402
ChainResidue
ATYR40
ATYR124
ATYR146
AARG181
ALEU211
ATYR215
AHIS265
AARG268
AFNR401
AHOH695

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
AGLU26
ALYS51
AHOH510
AHOH552

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FNR B 401
ChainResidue
BALA92
BPRO93
BILE94
BGLY95
BSER122
BGLN144
BTYR146
BTHR172
BLYS241
BSER263
BHIS265
BGLY266
BARG268
BASP296
BSER297
BGLY298
BARG300
BGLY319
BARG320
BPYR402
BHOH503
BHOH511
BHOH519
BHOH693

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYR B 402
ChainResidue
BTYR40
BTYR146
BARG181
BLEU211
BTYR215
BHIS265
BARG268
BFNR401
BHOH693

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 403
ChainResidue
BGLU26
BLYS51
BHOH510
BHOH529

site_idAC7
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FNR C 401
ChainResidue
CALA92
CPRO93
CILE94
CGLY95
CSER122
CGLN144
CTYR146
CTHR172
CLYS241
CSER263
CHIS265
CGLY266
CARG268
CASP296
CSER297
CGLY298
CVAL299
CARG300
CGLY319
CARG320
CPYR402
CHOH501
CHOH511
CHOH531

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR C 402
ChainResidue
CTYR40
CTYR146
CARG181
CLEU211
CHIS265
CARG268
CFNR401
CHOH735

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 403
ChainResidue
CGLU26
CLYS51
CHOH518
CHOH522

site_idBC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FNR D 401
ChainResidue
DALA92
DPRO93
DILE94
DGLY95
DSER122
DGLN144
DTYR146
DTHR172
DLYS241
DSER263
DHIS265
DGLY266
DARG268
DASP296
DSER297
DGLY298
DVAL299
DARG300
DGLY319
DARG320
DPYR402
DHOH502
DHOH506
DHOH541
DHOH634

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYR D 402
ChainResidue
DTYR40
DTYR124
DTYR146
DARG181
DLEU211
DTYR215
DHIS265
DARG268
DFNR401
DHOH634

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 Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"27302031","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues23
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_FI3
Number of Residues28
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_FI4
Number of Residues16
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_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17517371","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E77","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
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

250359

PDB entries from 2026-03-11

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