Structure of PDB 1c0p Chain A

Receptor sequence

>1c0pA (length=363) Species: 5286 (Rhodotorula toruloides)

LMMHSQKRVVVLGSGVIGLSSALILARKGYSVHILARDLPEDVSSQTFAS
PWAGANWTPFMTLTDGPRQAKWEESTFKKWVELVPTGHAMWLKGTRRFAQ
NEDGLLGHWYKDITPNYRPLPSSECPPGAIGVTYDTLSVHAPKYCQYLAR
ELQKLGATFERRTVTSLEQAFDGADLVVNATGLGAKSIAGIDDQAAEPIR
GQTVLVKSPCKRCTMDSSDPASPAYIIPRPGGEVICGGTYGVGDWDLSVN
PETVQRILKHCLRLDPTISSDGTIEGIEVLRHNVGLRPARRGGPRVEAER
IVLPLDRTKSPLSLGRGSARAAKEKEVTLVHAYGFSSAGYQQSWGAAEDV
AQLVDEAFQRYHG

3D structure

• PDB: 1c0p The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
• Chain: A
• Resolution: 1.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N1054 S1335 Q1339
• Catalytic site (residue number reindexed from 1): N56 S337 Q341
• Enzyme Commision number: 1.4.3.3: D-amino-acid oxidase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FAD	A	G1011 S1012 G1013 V1014 I1015 A1034 R1035 D1036 F1046 A1047 S1048 W1050 A1051 G1052 A1053 N1054 T1161 V1162 A1178 T1179 R1285 S1334 S1335 A1336 G1337 Y1338 Q1339	G13 S14 G15 V16 I17 A36 R37 D38 F48 A49 S50 W52 A53 G54 A55 N56 T163 V164 A180 T181 R287 S336 S337 A338 G339 Y340 Q341
BS02	DAL	A	F1058 Y1223 Y1238 R1285 S1335	F60 Y225 Y240 R287 S337

Gene Ontology

Molecular Function

• GO:0003884 D-amino-acid oxidase activity
• GO:0071949 FAD binding

Biological Process

• GO:0046416 D-amino acid metabolic process

External links

• PDB: RCSB:1c0p, PDBe:1c0p, PDBj:1c0p
• PDBsum: 1c0p
• PubMed: 11070076
• UniProt: P80324|OXDA_RHOTO D-amino-acid oxidase (Gene Name=DAO1)