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6A1N

Mandelate oxidase mutant-Y128F with (2R,3S)-3-fluoro-2-hydroxy-3-phenylpropanoic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004459molecular_functionL-lactate dehydrogenase activity
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016899molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor
A0017000biological_processantibiotic biosynthetic process
A0019516biological_processlactate oxidation
A0033072biological_processvancomycin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue FMN A 401
ChainResidue
ALEU25
AHIS252
AGLY253
AARG255
AASP283
AGLY285
AARG287
AGLY306
AARG307
A9O6404
AHOH581
AALA76
AHOH588
AHOH607
APRO77
AVAL78
AALA79
AGLN126
APHE128
ATHR154
ALYS228

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 402
ChainResidue
AARG162
AASP258
ASER288
AGLY290
AGLU331
AASP334
AHOH505
AHOH566
AHOH683

site_idAC3
Number of Residues8
Detailsbinding site for residue 9O6 A 403
ChainResidue
AALA41
AARG44
AVAL45
AILE264
AGLU265
ALYS353
ALEU354
AHOH760

site_idAC4
Number of Residues9
Detailsbinding site for residue 9O6 A 404
ChainResidue
AALA79
ATYR80
ALEU108
APHE128
AMET160
AARG163
AHIS252
AARG255
AFMN401

Functional Information from PROSITE/UniProt
site_idPS00557
Number of Residues7
DetailsFMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGGRQ
ChainResidueDetails
ASER250-GLN256

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683
ChainResidueDetails
AHIS252

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00683
ChainResidueDetails
AGLN126
APHE128
ATHR154
AARG163
ALYS228
AARG255
AASP283
AGLY306

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PDB entries from 2024-07-17

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