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5ZZY

The crystal structure of Mandelate oxidase mutant Y128F with L-Lactate

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 Residues21
Detailsbinding site for residue FMN A 401
ChainResidue
ALEU25
AHIS252
AARG255
AASP283
AGLY284
AGLY285
AARG287
AGLY306
AARG307
A2OP402
AHOH561
AALA76
AHOH572
AHOH632
APRO77
AVAL78
AALA79
AGLN126
APHE128
ATHR154
ALYS228

site_idAC2
Number of Residues4
Detailsbinding site for residue 2OP A 402
ChainResidue
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
APHE128
ATHR154
AARG163
ALYS228
AARG255
AASP283
AGLY306
AGLN126

218500

PDB entries from 2024-04-17

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