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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WET

Crystal structure of tryptophan 5-halogenase (PyrH) complex with FAD (tryptophan)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004497	molecular_function	monooxygenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0017000	biological_process	antibiotic biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0004497	molecular_function	monooxygenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0017000	biological_process	antibiotic biosynthetic process
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0004497	molecular_function	monooxygenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0017000	biological_process	antibiotic biosynthetic process
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0004497	molecular_function	monooxygenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0017000	biological_process	antibiotic biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 700

Chain	Residue
A	PRO352
A	THR356
A	GLY357
A	FAD1513

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 700

Chain	Residue
B	PRO352
B	THR356
B	GLY357
B	FAD1652

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL C 700

Chain	Residue
C	THR356
C	GLY357
C	FAD1513
C	HOH2109
C	PRO352

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL D 700

Chain	Residue
D	PRO352
D	THR356
D	GLY357
D	FAD1513
D	HOH2043

site_id	AC5
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD A 1513

Chain	Residue
A	GLY9
A	GLY10
A	GLY11
A	THR12
A	ALA13
A	GLU35
A	SER36
A	VAL39
A	ARG41
A	ILE42
A	VAL44
A	GLY45
A	ALA47
A	ASP193
A	ASP194
A	VAL195
A	CYS225
A	THR226
A	GLY227
A	ALA253
A	LEU345
A	PHE349
A	PRO352
A	GLY357
A	ILE358
A	ILE361
A	CL700
A	HOH2007
A	HOH2147
A	HOH2149
A	HOH2245
A	HOH2246
A	HOH2247
A	HOH2248
A	HOH2249
A	HOH2250
A	HOH2251

site_id	AC6
Number of Residues	32
Details	BINDING SITE FOR RESIDUE FAD B 1652

Chain	Residue
B	GLY9
B	GLY10
B	ALA13
B	SER36
B	VAL39
B	ARG41
B	ILE42
B	VAL44
B	GLY45
B	ALA47
B	VAL195
B	CYS225
B	THR226
B	GLY227
B	ARG229
B	TRP281
B	ILE283
B	GLY344
B	LEU345
B	PHE349
B	PRO352
B	SER355
B	GLY357
B	ILE358
B	ILE361
B	CL700
B	HOH2202
B	HOH2203
B	HOH2204
B	HOH2205
B	HOH2206
B	HOH2207

site_id	AC7
Number of Residues	39
Details	BINDING SITE FOR RESIDUE FAD C 1513

Chain	Residue
C	ASP193
C	VAL195
C	CYS225
C	THR226
C	GLY227
C	ARG229
C	LEU231
C	ALA253
C	GLY344
C	LEU345
C	PHE349
C	PRO352
C	GLY357
C	ILE358
C	ILE361
C	CL700
C	HOH2002
C	HOH2006
C	HOH2062
C	HOH2108
C	HOH2110
C	HOH2177
C	HOH2178
C	HOH2179
C	HOH2180
C	HOH2181
C	HOH2182
C	GLY9
C	GLY10
C	GLY11
C	THR12
C	ALA13
C	SER36
C	VAL39
C	ARG41
C	ILE42
C	VAL44
C	GLY45
C	ALA47

site_id	AC8
Number of Residues	33
Details	BINDING SITE FOR RESIDUE FAD D 1513

Chain	Residue
D	GLY9
D	GLY10
D	GLY11
D	THR12
D	ALA13
D	SER36
D	VAL39
D	ARG41
D	ILE42
D	VAL44
D	GLY45
D	ALA47
D	ASP193
D	VAL195
D	CYS225
D	THR226
D	GLY227
D	ARG229
D	ALA253
D	TRP281
D	GLY344
D	LEU345
D	PHE349
D	PRO352
D	GLY357
D	ILE358
D	ILE361
D	CL700
D	HOH2040
D	HOH2102
D	HOH2103
D	HOH2104
D	HOH2105

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 1514

Chain	Residue
C	ARG240
C	ARG334
C	ARG334
C	SER383
C	ASN386
C	HOH2069
C	HOH2183

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL D 1514

Chain	Residue
A	HOH2208
D	LYS370

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 1514

Chain	Residue
A	LYS370
D	HOH2082

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 1653

Chain	Residue
B	ALA158

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 1515

Chain	Residue
C	LYS370

site_id	BC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE TRP B 650

Chain	Residue
B	PHE49
B	SER50
B	THR51
B	ILE78
B	HIS92
B	PRO93
B	PHE94
B	GLN160
B	GLN163
B	GLU354
B	GLY450
B	PHE451
B	TYR454
B	HOH2180

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000250\|UniProtKB:P95480

Chain	Residue	Details
A	LYS75
B	LYS75
C	LYS75
D	LYS75

site_id	SWS_FT_FI2
Number of Residues	44
Details	BINDING: BINDING => ECO:0000269\|PubMed:19501593, ECO:0007744\|PDB:2WES, ECO:0007744\|PDB:2WET

Chain	Residue	Details
A	GLY10
A	GLY357
A	ILE358
B	GLY10
B	ALA13
B	SER36
B	VAL39
B	ILE42
B	ALA47
B	VAL195
B	LEU345
A	ALA13
B	THR356
B	GLY357
B	ILE358
C	GLY10
C	ALA13
C	SER36
C	VAL39
C	ILE42
C	ALA47
C	VAL195
A	SER36
C	LEU345
C	THR356
C	GLY357
C	ILE358
D	GLY10
D	ALA13
D	SER36
D	VAL39
D	ILE42
D	ALA47
A	VAL39
D	VAL195
D	LEU345
D	THR356
D	GLY357
D	ILE358
A	ILE42
A	ALA47
A	VAL195
A	LEU345
A	THR356

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:19501593, ECO:0007744\|PDB:2WET

Chain	Residue	Details
A	VAL44
B	VAL44
C	VAL44
D	VAL44

site_id	SWS_FT_FI4
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:19501593, ECO:0007744\|PDB:2WET, ECO:0007744\|PDB:2WEU

Chain	Residue	Details
A	SER50
B	GLN163
B	GLY450
B	TYR454
C	SER50
C	PRO93
C	GLN160
C	GLN163
C	GLY450
C	TYR454
D	SER50
A	PRO93
D	PRO93
D	GLN160
D	GLN163
D	GLY450
D	TYR454
A	GLN160
A	GLN163
A	GLY450
A	TYR454
B	SER50
B	PRO93
B	GLN160

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Important for activity => ECO:0000250\|UniProtKB:P95480

Chain	Residue	Details
A	GLU354
B	GLU354
C	GLU354
D	GLU354

222036

PDB entries from 2024-07-03

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