6LYH

Crystal structure of tea N9-methyltransferase CkTcS in complex with SAH and 1,3,7-trimethyluric acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008168	molecular_function	methyltransferase activity
B	0008168	molecular_function	methyltransferase activity
C	0008168	molecular_function	methyltransferase activity
D	0008168	molecular_function	methyltransferase activity
E	0008168	molecular_function	methyltransferase activity
F	0008168	molecular_function	methyltransferase activity
G	0008168	molecular_function	methyltransferase activity
H	0008168	molecular_function	methyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue SAH B 501

Chain	Residue
B	MET15
B	LEU105
B	GLY138
B	SER139
B	PHE140
B	HIS141
B	SER156
B	TYR157
B	SER158
B	TYR24
B	THR31
B	GLY66
B	CYS67
B	ALA68
B	ASN72
B	ASN103
B	ASP104

---

site_id	AC2
Number of Residues	8
Details	binding site for residue EXU B 502

Chain	Residue
B	PHE30
B	THR31
B	HIS160
B	TRP161
B	ARG226
B	PHE272
B	ILE318
B	PHE322

---

site_id	AC3
Number of Residues	16
Details	binding site for residue SAH A 501

Chain	Residue
A	MET15
A	TYR24
A	THR31
A	GLY66
A	ALA68
A	ASN72
A	ASN103
A	ASP104
A	LEU105
A	GLY138
A	SER139
A	PHE140
A	HIS141
A	SER156
A	TYR157
A	SER158

---

site_id	AC4
Number of Residues	11
Details	binding site for residue EXU A 502

Chain	Residue
A	MET15
A	TYR24
A	PHE30
A	THR31
A	TYR157
A	HIS160
A	TRP161
A	ARG226
A	PHE272
A	ILE318
A	PHE322

---

site_id	AC5
Number of Residues	12
Details	binding site for residue SAH C 501

Chain	Residue
C	LEU13
C	MET15
C	GLY66
C	ALA68
C	ASP104
C	LEU105
C	SER139
C	PHE140
C	HIS141
C	TYR157
C	SER158
C	TRP161

---

site_id	AC6
Number of Residues	9
Details	binding site for residue EXU C 502

Chain	Residue
C	TYR24
C	PHE30
C	THR31
C	TYR157
C	HIS160
C	TRP161
C	ARG226
C	ILE318
C	PHE322

---

site_id	AC7
Number of Residues	19
Details	binding site for residue SAH D 501

Chain	Residue
D	LEU13
D	MET15
D	TYR24
D	THR31
D	GLY66
D	CYS67
D	ALA68
D	ASN72
D	ASP104
D	LEU105
D	GLY138
D	SER139
D	PHE140
D	HIS141
D	SER156
D	TYR157
D	SER158
D	TRP161
D	EXU502

---

site_id	AC8
Number of Residues	11
Details	binding site for residue EXU D 502

Chain	Residue
D	PHE272
D	ILE318
D	PHE322
D	SAH501
D	TYR24
D	PHE30
D	THR31
D	TYR157
D	HIS160
D	TRP161
D	ARG226

---

site_id	AC9
Number of Residues	18
Details	binding site for residue SAH E 501

Chain	Residue
E	LEU13
E	PHE14
E	MET15
E	TYR24
E	THR31
E	GLY66
E	ALA68
E	ASN72
E	ASP104
E	LEU105
E	GLY138
E	SER139
E	PHE140
E	HIS141
E	SER156
E	TYR157
E	SER158
E	TRP161

---

site_id	AD1
Number of Residues	10
Details	binding site for residue EXU E 502

Chain	Residue
E	TYR24
E	PHE30
E	THR31
E	TYR157
E	HIS160
E	TRP161
E	ARG226
E	PHE272
E	ILE318
E	PHE322

---

site_id	AD2
Number of Residues	11
Details	binding site for residue SAH F 501

Chain	Residue
F	PHE14
F	MET15
F	ALA68
F	ASP104
F	LEU105
F	GLY138
F	SER139
F	PHE140
F	HIS141
F	TYR157
F	SER158

---

site_id	AD3
Number of Residues	7
Details	binding site for residue EXU F 502

Chain	Residue
F	TYR24
F	PHE30
F	THR31
F	TYR157
F	ARG226
F	PHE272
F	ILE318

---

site_id	AD4
Number of Residues	16
Details	binding site for residue SAH G 501

Chain	Residue
G	LEU13
G	MET15
G	TYR24
G	THR31
G	GLY66
G	ALA68
G	ASN72
G	ASP104
G	LEU105
G	GLY138
G	SER139
G	PHE140
G	HIS141
G	SER156
G	TYR157
G	SER158

---

site_id	AD5
Number of Residues	11
Details	binding site for residue EXU G 502

Chain	Residue
G	MET15
G	TYR24
G	PHE30
G	THR31
G	TYR157
G	HIS160
G	TRP161
G	ARG226
G	PHE272
G	ILE318
G	PHE322

---

site_id	AD6
Number of Residues	18
Details	binding site for residue SAH H 501

Chain	Residue
H	LEU13
H	MET15
H	TYR24
H	THR31
H	GLY66
H	CYS67
H	ALA68
H	ASN72
H	THR73
H	ASP104
H	LEU105
H	SER139
H	PHE140
H	HIS141
H	SER156
H	TYR157
H	SER158
H	EXU502

---

site_id	AD7
Number of Residues	7
Details	binding site for residue EXU H 502

Chain	Residue
H	TYR24
H	PHE30
H	THR31
H	HIS160
H	TRP161
H	PHE322
H	SAH501

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250|UniProtKB:A4GE70

Chain	Residue	Details
B	TYR24
A	TYR24
C	TYR24
D	TYR24
E	TYR24
F	TYR24
G	TYR24
H	TYR24

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	BINDING: BINDING => ECO:0000250|UniProtKB:A4GE69

Chain	Residue	Details
B	ASN27
C	GLY66
C	SER156
C	TYR157
D	ASN27
D	GLY66
D	SER156
D	TYR157
E	ASN27
E	GLY66
E	SER156
B	GLY66
E	TYR157
F	ASN27
F	GLY66
F	SER156
F	TYR157
G	ASN27
G	GLY66
G	SER156
G	TYR157
H	ASN27
B	SER156
H	GLY66
H	SER156
H	TYR157
B	TYR157
A	ASN27
A	GLY66
A	SER156
A	TYR157
C	ASN27

---

site_id	SWS_FT_FI3
Number of Residues	32
Details	BINDING: BINDING => ECO:0000250|UniProtKB:A0A6C0WW36

Chain	Residue	Details
B	CYS67
C	ASN72
C	MET102
C	SER139
D	CYS67
D	ASN72
D	MET102
D	SER139
E	CYS67
E	ASN72
E	MET102
B	ASN72
E	SER139
F	CYS67
F	ASN72
F	MET102
F	SER139
G	CYS67
G	ASN72
G	MET102
G	SER139
H	CYS67
B	MET102
H	ASN72
H	MET102
H	SER139
B	SER139
A	CYS67
A	ASN72
A	MET102
A	SER139
C	CYS67

---

site_id	SWS_FT_FI4
Number of Residues	32
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9FLN8

Chain	Residue	Details
B	ASN178
C	ASP264
C	PHE266
C	ASN267
D	ASN178
D	ASP264
D	PHE266
D	ASN267
E	ASN178
E	ASP264
E	PHE266
B	ASP264
E	ASN267
F	ASN178
F	ASP264
F	PHE266
F	ASN267
G	ASN178
G	ASP264
G	PHE266
G	ASN267
H	ASN178
B	PHE266
H	ASP264
H	PHE266
H	ASN267
B	ASN267
A	ASN178
A	ASP264
A	PHE266
A	ASN267
C	ASN178

---

site_id	SWS_FT_FI5
Number of Residues	16
Details	SITE: Involved in substrate discrimination => ECO:0000269|PubMed:27116373

Chain	Residue	Details
B	HIS154
E	HIS333
F	HIS154
F	HIS333
G	HIS154
G	HIS333
H	HIS154
H	HIS333
B	HIS333
A	HIS154
A	HIS333
C	HIS154
C	HIS333
D	HIS154
D	HIS333
E	HIS154

---

site_id	SWS_FT_FI6
Number of Residues	16
Details	SITE: Involved in substrate discrimination => ECO:0000269|PubMed:25133732

Chain	Residue	Details
B	ARG226
E	ILE318
F	ARG226
F	ILE318
G	ARG226
G	ILE318
H	ARG226
H	ILE318
B	ILE318
A	ARG226
A	ILE318
C	ARG226
C	ILE318
D	ARG226
D	ILE318
E	ARG226

---

site_id	SWS_FT_FI7
Number of Residues	8
Details	SITE: Involved in substrate discrimination => ECO:0000269|PubMed:26773541

Chain	Residue	Details
B	CYS270
A	CYS270
C	CYS270
D	CYS270
E	CYS270
F	CYS270
G	CYS270
H	CYS270

---