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6A08

The crystal structure of Mandelate oxidase with benzoyl-formic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0016899molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor
A0017000biological_processantibiotic biosynthetic process
A0033072biological_processvancomycin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 401
ChainResidue
AGLY284
AGLY285
AILE286
ALEU304
AFMN402

site_idAC2
Number of Residues21
Detailsbinding site for residue FMN A 402
ChainResidue
AALA79
AGLN126
ATYR128
ATHR154
ALYS228
AHIS252
AGLY253
AARG255
AASP283
AGLY285
AARG287
AGLY306
AARG307
AMG401
A173404
AHOH575
AHOH610
ALEU25
AALA76
APRO77
AVAL78

site_idAC3
Number of Residues5
Detailsbinding site for residue 173 A 403
ChainResidue
AVAL157
ATRP159
AMET160
APHE206
AHOH660

site_idAC4
Number of Residues9
Detailsbinding site for residue 173 A 404
ChainResidue
AALA79
ATYR80
ALEU108
ATYR128
AMET160
AARG163
AHIS252
AARG255
AFMN402

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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