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8UFY

High Resolution structure of A. viridans Lactate Oxidase

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:27302031
ChainResidueDetails
AHIS265
BHIS265

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:17517371, ECO:0000269|PubMed:25423902, ECO:0007744|PDB:2E77, ECO:0007744|PDB:4RJE
ChainResidueDetails
ATYR40
BTYR215
BHIS265
BARG268
ATYR146
AARG181
ATYR215
AHIS265
AARG268
BTYR40
BTYR146
BARG181

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17517371, ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2DU2, ECO:0007744|PDB:2E77, ECO:0007744|PDB:2NLI
ChainResidueDetails
APRO93
AASP296
AARG320
BPRO93
BASP296
BARG320

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17517371, ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2E77, ECO:0007744|PDB:2NLI
ChainResidueDetails
ASER122
ATHR172
ALYS241
ASER263
BSER122
BTHR172
BLYS241
BSER263

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17517371, ECO:0007744|PDB:2E77
ChainResidueDetails
AGLN144
BGLN144

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Is suggested to participate in control of opening/closing motions of the active-site lid in A.viridans LOX => ECO:0000305|PubMed:27302031
ChainResidueDetails
ATYR215
BTYR215

223790

PDB entries from 2024-08-14

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