1C0L

D-AMINO ACID OXIDASE: STRUCTURE OF SUBSTRATE COMPLEXES AT VERY HIGH RESOLUTION REVEAL THE CHEMICAL REACTTION MECHANISM OF FLAVIN DEHYDROGENATION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003884	molecular_function	D-amino-acid oxidase activity
A	0046416	biological_process	D-amino acid metabolic process
A	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FLA A 1364

Chain	Residue
A	ASN1054
A	HOH2167
A	PHE1058
A	MET1213
A	TYR1223
A	TYR1238
A	ARG1285
A	SER1335
A	FAD1363
A	HOH2071

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site_id	AC2
Number of Residues	38
Details	BINDING SITE FOR RESIDUE FAD A 1363

Chain	Residue
A	GLY1011
A	SER1012
A	GLY1013
A	VAL1014
A	ILE1015
A	ALA1034
A	ARG1035
A	ASP1036
A	PHE1046
A	ALA1047
A	SER1048
A	TRP1050
A	ALA1051
A	GLY1052
A	ALA1053
A	ASN1054
A	ARG1160
A	THR1161
A	VAL1162
A	ALA1178
A	THR1179
A	GLY1182
A	ILE1186
A	THR1201
A	PRO1286
A	SER1334
A	SER1335
A	ALA1336
A	GLY1337
A	TYR1338
A	GLN1339
A	FLA1364
A	HOH2001
A	HOH2002
A	HOH2008
A	HOH2009
A	HOH2035
A	HOH2039

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Functional Information from PROSITE/UniProt

site_id	PS00677
Number of Residues	19
Details	DAO D-amino acid oxidases signature. LVHAYGfSSaGyqqswGaA

Chain	Residue	Details
A	LEU1327-ALA1345

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	13
Details	BINDING: BINDING => ECO:0000269|PubMed:11070076, ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, ECO:0007744|PDB:1C0P

Chain	Residue	Details
A	SER1012
A	SER1334
A	SER1335
A	TYR1338
A	GLN1339
A	ILE1015
A	ARG1035
A	ASP1036
A	SER1048
A	GLY1052
A	ASN1054
A	VAL1162
A	ARG1285

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11070076, ECO:0007744|PDB:1C0K, ECO:0007744|PDB:1C0L, ECO:0007744|PDB:1C0P

Chain	Residue	Details
A	ALA1047

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I

Chain	Residue	Details
A	PHE1058
A	TYR1223
A	TYR1238

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11070076, ECO:0000269|PubMed:12445787, ECO:0007744|PDB:1C0I, ECO:0007744|PDB:1C0L, ECO:0007744|PDB:1C0P

Chain	Residue	Details
A	GLY1337

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498

Chain	Residue	Details
A	ASN1177

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1c0k

Chain	Residue	Details
A	SER1335

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site_id	MCSA1
Number of Residues	3
Details	M-CSA 110

Chain	Residue	Details
A	ASN1054	modifies pKa
A	SER1335	hydrogen bond acceptor, hydrogen bond donor, modifies pKa
A	GLN1339	hydrogen bond acceptor, modifies pKa

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