4R29

Crystal structure of bacterial cysteine methyltransferase effector NleE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0008168	molecular_function	methyltransferase activity
A	0032259	biological_process	methylation
A	0035821	biological_process	modulation of process of another organism
A	0042025	cellular_component	host cell nucleus
A	0090729	molecular_function	toxin activity
B	0005576	cellular_component	extracellular region
B	0008168	molecular_function	methyltransferase activity
B	0032259	biological_process	methylation
B	0035821	biological_process	modulation of process of another organism
B	0042025	cellular_component	host cell nucleus
B	0090729	molecular_function	toxin activity
C	0005576	cellular_component	extracellular region
C	0008168	molecular_function	methyltransferase activity
C	0032259	biological_process	methylation
C	0035821	biological_process	modulation of process of another organism
C	0042025	cellular_component	host cell nucleus
C	0090729	molecular_function	toxin activity
D	0005576	cellular_component	extracellular region
D	0008168	molecular_function	methyltransferase activity
D	0032259	biological_process	methylation
D	0035821	biological_process	modulation of process of another organism
D	0042025	cellular_component	host cell nucleus
D	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SAM A 301

Chain	Residue
A	ARG89
A	GLY199
A	PHE202
A	TYR204
A	GLU208
A	TYR212
A	GOL302
A	HOH406
A	HOH425
A	ALA92
A	SER98
A	ARG107
A	GLY110
A	GLN111
A	GLU191
A	ALA195
A	MET198

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	ARG89
A	SER93
A	PRO95
A	GLN111
A	PHE112
A	SER113
A	SAM301

---

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE SAM B 301

Chain	Residue
A	ASN179
B	ARG89
B	ALA92
B	SER98
B	ARG107
B	GLY110
B	GLN111
B	GLU191
B	ALA195
B	MET198
B	GLY199
B	PHE202
B	TYR204
B	GLU208
B	TYR212
B	CIT302

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT B 302

Chain	Residue
B	ARG89
B	ALA92
B	SER93
B	PRO95
B	GLN111
B	PHE112
B	SER113
B	SAM301

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SAM C 301

Chain	Residue
C	ARG89
C	ALA92
C	SER98
C	ARG107
C	GLY110
C	GLN111
C	GLU191
C	ALA195
C	MET198
C	GLY199
C	PHE202
C	TYR204
C	GLU208
C	TYR212
C	CIT302
C	GOL303
C	HOH454

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT C 302

Chain	Residue
C	GLN111
C	LYS138
C	ILE146
C	TYR168
C	GLU191
C	MET198
C	SAM301
C	HOH451

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 303

Chain	Residue
C	ALA92
C	SER93
C	THR94
C	PRO95
C	SER98
C	SAM301
C	HOH451

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE SAM D 301

Chain	Residue
D	ARG89
D	ALA92
D	SER98
D	ARG107
D	GLY110
D	GLN111
D	GLU191
D	ILE194
D	ALA195
D	MET198
D	GLY199
D	PHE202
D	TYR204
D	GLU208
D	TYR212
D	GOL302

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 302

Chain	Residue
D	MET198
D	SAM301
D	GLN111
D	LYS171
D	GLU191

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:25412445, ECO:0007744|PDB:4R29

Chain	Residue	Details
A	ALA92
B	GLN111
B	TYR204
B	GLU208
C	ALA92
C	SER98
C	ARG107
C	GLN111
C	TYR204
C	GLU208
D	ALA92
A	SER98
D	SER98
D	ARG107
D	GLN111
D	TYR204
D	GLU208
A	ARG107
A	GLN111
A	TYR204
A	GLU208
B	ALA92
B	SER98
B	ARG107

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