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6A1L

Mandelate oxidase mutant-Y128F with 5-deazariboflavin mononucleotide and benzoic 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 9O9 A 401
ChainResidue
ALEU25
ALYS228
AHIS252
AARG255
AASP283
AGLY284
AGLY285
AARG287
AGLY306
AARG307
AMG402
AALA76
ABEZ403
AHOH571
APRO77
AVAL78
AALA79
ACYS106
AGLN126
APHE128
ATHR154

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 402
ChainResidue
AGLY284
AGLY285
AILE286
ALEU304
A9O9401

site_idAC3
Number of Residues8
Detailsbinding site for residue BEZ A 403
ChainResidue
APHE24
AALA79
ALEU108
AMET160
AARG163
AHIS252
AARG255
A9O9401

site_idAC4
Number of Residues4
Detailsbinding site for residue BEZ A 404
ChainResidue
AALA41
AVAL45
AGLU265
ALYS353

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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