Structure of PDB 5zzz Chain A Binding Site BS01

Receptor Information

>5zzz Chain A (length=332) Species: 31958 (Amycolatopsis orientalis)

YVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRML
RDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVP
YTICTLSSVSLEEIAAVGGRPWFQLCWLRDEKRSLDLVRRAEDAGCEAIV
FTVDVPWMGRRLRDMRNGFALPEWVTAANFFAPATWESVEAVRAHTDLPV
VLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVS
GGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLL
ELLAEEVRDAMGLAGCESVGAARRLNTKLGVV

Ligand information

• Ligand ID: FMN
• InChI: InChI=1S/C17H21N4O9P/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t11-,12+,14-/m0/s1
• InChIKey: FVTCRASFADXXNN-SCRDCRAPSA-N
• SMILES:
  OpenEye OEToolkits 1.7.6: Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)O)O)O)O
  OpenEye OEToolkits 1.7.6: Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O
  ACDLabs 12.01: N=2C(=O)NC(=O)C3=Nc1cc(C)c(C)cc1N(C=23)CC(O)C(O)C(O)COP(=O)(O)O
  CACTVS 3.385: Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O)c2cc1C
  CACTVS 3.385: Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O)c2cc1C
• Formula: C17 H21 N4 O9 P
• Name: FLAVIN MONONUCLEOTIDE;
  RIBOFLAVIN MONOPHOSPHATE
• ChEMBL: CHEMBL1201794
• DrugBank: DB03247
• ZINC: ZINC000003831425
• PDB chain: 5zzz Chain A Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5zzz The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.
• Resolution: 1.446 Å
• Binding residue (original residue number in PDB): P77 V78 A79 Q126 T154 K228 H252 G253 R255 D283 G285 R287 G306 R307
• Binding residue (residue number reindexed from 1): P75 V76 A77 Q124 T152 K203 H227 G228 R230 D258 G260 R262 G281 R282
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): C128 D156 H252
• Catalytic site (residue number reindexed from 1): C126 D154 H227
• Enzyme Commision number: 1.1.3.46: 4-hydroxymandelate oxidase.

Gene Ontology

Molecular Function

• GO:0004459 L-lactate dehydrogenase activity
• GO:0010181 FMN binding
• GO:0016491 oxidoreductase activity
• GO:0016899 oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor

Biological Process

• GO:0017000 antibiotic biosynthetic process
• GO:0033072 vancomycin biosynthetic process

External links

• PDB: RCSB:5zzz, PDBe:5zzz, PDBj:5zzz
• PDBsum: 5zzz
• PubMed: 31588923
• UniProt: O52792|HMO_AMYOR 4-hydroxymandelate oxidase (Gene Name=hmo)