2WEU

Crystal structure of tryptophan 5-halogenase (PyrH) complex with substrate 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	13
Details	BINDING SITE FOR RESIDUE TRP A 1512

Chain	Residue
A	PHE49
A	GLY450
A	TYR454
A	HOH2114
A	HOH2341
A	SER50
A	THR51
A	HIS92
A	PRO93
A	PHE94
A	GLN160
A	GLN163
A	GLU354

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TRP B 1512

Chain	Residue
B	PHE49
B	SER50
B	THR51
B	HIS92
B	PRO93
B	PHE94
B	GLN160
B	GLN163
B	GLU354
B	GLY450
B	PHE451
B	TYR454
B	HOH2105
B	HOH2112
B	HOH2341

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE TRP C 1512

Chain	Residue
C	PHE49
C	SER50
C	THR51
C	HIS92
C	PRO93
C	PHE94
C	GLN160
C	GLN163
C	GLU354
C	GLY450
C	TYR454
C	HOH2115
C	HOH2332
C	HOH2336

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE TRP D 1512

Chain	Residue
D	PHE49
D	SER50
D	THR51
D	HIS92
D	PRO93
D	PHE94
D	GLN160
D	GLN163
D	GLU354
D	GLY450
D	PHE451
D	TYR454
D	HOH2091
D	HOH2095

---

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

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