Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WJ6

CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) FROM ARTHROBACTER NITROGUAJACOLICUS RU61A COMPLEXED WITH ITS NATURAL PRODUCT N- ACETYLANTHRANILATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016491	molecular_function	oxidoreductase activity
A	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A	0019335	biological_process	methylquinoline catabolic process
A	0050586	molecular_function	3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity
A	0051213	molecular_function	dioxygenase activity
B	0003824	molecular_function	catalytic activity
B	0016491	molecular_function	oxidoreductase activity
B	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B	0019335	biological_process	methylquinoline catabolic process
B	0050586	molecular_function	3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity
B	0051213	molecular_function	dioxygenase activity
C	0003824	molecular_function	catalytic activity
C	0016491	molecular_function	oxidoreductase activity
C	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
C	0019335	biological_process	methylquinoline catabolic process
C	0050586	molecular_function	3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity
C	0051213	molecular_function	dioxygenase activity
D	0003824	molecular_function	catalytic activity
D	0016491	molecular_function	oxidoreductase activity
D	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
D	0019335	biological_process	methylquinoline catabolic process
D	0050586	molecular_function	3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase activity
D	0051213	molecular_function	dioxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1276

Chain	Residue
A	ALA235
A	PHE241
A	K1282
D	ASP158
D	ASP162
D	GLY163

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 1275

Chain	Residue
C	HOH2214
C	ASP53
C	ARG273
C	HOH2048

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 1275

Chain	Residue
D	THR4
D	TYR5
D	ALA207
D	HIS238

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1276

Chain	Residue
B	THR2
B	PHE234
B	HIS238

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 1276

Chain	Residue
B	ALA235
B	PHE241
B	TYR243
B	K1281
B	HOH2158
C	ASP158

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1277

Chain	Residue
A	TRP149
A	ARG150
A	HOH2170

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1278

Chain	Residue
A	LEU128
A	TRP130
A	ALA131
A	PRO132
A	LYS133
A	PHE136
A	TYR196
A	GOL1279

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1279

Chain	Residue
A	LEU128
A	PHE136
A	VAL159
A	TRP160
A	GOL1278
A	HOH2141
A	HOH2173

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1280

Chain	Residue
A	LYS245
A	LEU246
A	GLY247
A	GOL1281

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1281

Chain	Residue
A	LYS245
A	GOL1280
A	HOH2171
D	HIS164
D	ASP165
D	GLU166
D	HOH2093

site_id	BC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GOL C 1277

Chain	Residue
C	SER101
C	HIS102
C	ASP126
C	TRP127
C	LEU128
C	PHE136
C	TRP160
C	HIS251
C	ZZ81280
C	HOH2100
C	HOH2173
C	HOH2215

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1277

Chain	Residue
B	LYS245
B	LEU246
B	GLY247
B	GOL1280
B	HOH2181

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL D 1276

Chain	Residue
D	SER101
D	HIS102
D	ASP126
D	TRP127
D	LEU128
D	PHE136
D	TRP160
D	HIS251
D	ZZ81278
D	HOH2125

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 1278

Chain	Residue
C	GLY75
C	TYR76
C	GLN77
C	VAL191
C	ASP194
C	ALA195

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 1278

Chain	Residue
B	HIS164
B	ASP165
B	GOL1279
B	HOH2110
B	HOH2184
D	LYS245
D	LEU246
D	GLY247

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 1279

Chain	Residue
B	GOL1278
B	HOH2185
D	GLY247

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1280

Chain	Residue
C	ASP165
C	GLU166
B	LYS245
B	GOL1277
C	HIS164

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 1279

Chain	Residue
C	ALA235
C	HIS238
C	PHE241
C	HOH2184
C	HOH2185
C	HOH2191

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K A 1282

Chain	Residue
A	ALA235
A	HIS238
A	PRO239
A	PHE241
A	GOL1276
A	HOH2169
D	HOH2086

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K D 1277

Chain	Residue
D	ALA235
D	HIS238
D	PRO239
D	PHE241
D	HOH2134
D	HOH2137

site_id	CC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K B 1281

Chain	Residue
B	ALA235
B	HIS238
B	PRO239
B	PHE241
B	HOH2158
C	GOL1276
C	HOH2126

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A 1283

Chain	Residue
A	ASP165
A	SRT1286
A	HOH2099

site_id	CC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ZZ8 A 1284

Chain	Residue
A	TRP36
A	HIS38
A	HIS100
A	SER101
A	HIS102
A	TRP160
A	TRP185
A	SER188
A	ILE192
A	HIS251
A	HOH2172
A	HOH2173

site_id	CC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ZZ8 B 1282

Chain	Residue
B	TRP36
B	HIS38
B	HIS100
B	SER101
B	HIS102
B	TRP160
B	TRP185
B	SER188
B	ILE192
B	HIS251
B	HOH2188

site_id	CC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ZZ8 C 1280

Chain	Residue
C	TRP36
C	HIS38
C	HIS100
C	SER101
C	HIS102
C	TRP160
C	TRP185
C	SER188
C	ILE192
C	HIS251
C	GOL1277
C	HOH2036

site_id	CC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ZZ8 D 1278

Chain	Residue
D	TRP36
D	HIS38
D	HIS100
D	SER101
D	HIS102
D	TRP160
D	TRP185
D	SER188
D	ILE192
D	HIS251
D	GOL1276

site_id	CC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SRT A 1285

Chain	Residue
A	LYS167
A	ARG170
A	HIS171
A	HOH2175
A	HOH2176
C	ARG260
C	VAL263

site_id	DC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SRT B 1283

Chain	Residue
B	LYS167
B	ARG170
B	HIS171
B	HOH2189
B	HOH2190
D	ARG260
D	VAL263

site_id	DC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SRT C 1281

Chain	Residue
B	ARG260
B	VAL263
C	LYS167
C	ARG170
C	HIS171
C	HOH2216

site_id	DC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SRT D 1279

Chain	Residue
A	ARG260
A	VAL263
D	LYS167
D	ARG170
D	HIS171
D	HOH2156

site_id	DC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SRT A 1286

Chain	Residue
A	HIS164
A	ASP165
A	K1283
A	HOH2177
A	HOH2178
A	HOH2179
C	LYS245
C	LEU246
C	GLY247

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	488
Details	Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"16187153","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Increases basicity of active site His","evidences":[{"source":"UniProtKB","id":"B1MFK2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)