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6A0B

The crystal structure of Mandelate oxidase mutant Y128F with (R)-3,3,3-trifluoro-2-hydroxy-propionic 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 Residues21
Detailsbinding site for residue FMN A 401
ChainResidue
ALEU25
ALYS228
AHIS252
AARG255
AASP283
AGLY284
AGLY285
AARG287
AGLY306
AARG307
A9O0402
AALA76
AHOH549
AHOH642
APRO77
AVAL78
AALA79
ACYS106
AGLN126
APHE128
ATHR154

site_idAC2
Number of Residues8
Detailsbinding site for residue 9O0 A 402
ChainResidue
APHE128
AMET160
AARG163
APHE206
AHIS252
AARG255
AFMN401
AHOH871

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

239803

PDB entries from 2025-08-06

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