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6A0G

The crystal structure of Mandelate oxidase mutant Y128F with b-Phenyllactate

Functional Information from GO Data
ChainGOidnamespacecontents
A0001561biological_processfatty acid alpha-oxidation
A0004459molecular_functionL-lactate dehydrogenase activity
A0005777cellular_componentperoxisome
A0005886cellular_componentplasma membrane
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 Residues20
Detailsbinding site for residue FMN A 401
ChainResidue
ALEU25
AHIS252
AARG255
AASP283
AGLY285
AARG287
AGLY306
AARG307
AHFA402
AHOH533
AHOH534
AALA76
AHOH625
APRO77
AVAL78
AALA79
AGLN126
APHE128
ATHR154
ALYS228

site_idAC2
Number of Residues6
Detailsbinding site for residue HFA A 402
ChainResidue
APHE24
ALEU108
AMET160
AHIS252
AARG255
AFMN401

site_idAC3
Number of Residues7
Detailsbinding site for residue HFA A 403
ChainResidue
AALA41
AVAL45
AILE264
AGLU265
ALYS353
AHOH555
AHOH690

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
APHE128
ATHR154
AARG163
ALYS228
AARG255
AASP283
AGLY306
AGLN126

218500

数据于2024-04-17公开中

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