3FTQ

Crystal structure of Septin 2 in complex with GppNHp and Mg2+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005525	molecular_function	GTP binding
A	0051301	biological_process	cell division
B	0005525	molecular_function	GTP binding
B	0051301	biological_process	cell division
C	0005525	molecular_function	GTP binding
C	0051301	biological_process	cell division
D	0005525	molecular_function	GTP binding
D	0051301	biological_process	cell division

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 371

Chain	Residue
A	SER51
A	THR78
A	HOH320
A	HOH321
A	GNP372

---

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GNP A 372

Chain	Residue
A	LYS50
A	SER51
A	THR52
A	THR78
A	GLY104
A	LYS183
A	ASP185
A	VAL240
A	GLY241
A	ARG256
A	TYR258
A	HOH310
A	HOH320
A	HOH321
A	MG371
B	THR186
B	GLU191
A	SER46
A	GLY47
A	LEU48
A	GLY49

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 371

Chain	Residue
B	HOH6
B	HOH27
B	SER51
B	THR78
B	GNP372

---

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GNP B 372

Chain	Residue
A	THR186
A	GLU191
B	HOH6
B	HOH27
B	SER46
B	GLY47
B	LEU48
B	GLY49
B	LYS50
B	SER51
B	THR52
B	ARG77
B	THR78
B	GLY104
B	LYS183
B	ASP185
B	VAL240
B	GLY241
B	ARG256
B	TYR258
B	HOH326
B	MG371

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 371

Chain	Residue
C	SER51
C	THR78
C	HOH315
C	HOH318
C	GNP372

---

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GNP C 372

Chain	Residue
C	SER46
C	GLY47
C	LEU48
C	GLY49
C	LYS50
C	SER51
C	THR52
C	ARG77
C	THR78
C	GLY104
C	LYS183
C	ASP185
C	VAL240
C	GLY241
C	ARG256
C	TYR258
C	HOH315
C	HOH318
C	MG371
D	THR186
D	GLU191

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 371

Chain	Residue
D	HOH5
D	SER51
D	THR78
D	HOH317
D	GNP372

---

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GNP D 372

Chain	Residue
D	VAL240
D	GLY241
D	ARG256
D	HOH307
D	HOH317
D	MG371
C	THR186
C	GLU191
D	HOH5
D	SER46
D	GLY47
D	LEU48
D	GLY49
D	LYS50
D	SER51
D	THR52
D	ARG77
D	THR78
D	GLY104
D	LYS183
D	ASP185

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING:

Chain	Residue	Details
B	LYS183
B	ARG256
C	GLY44
C	THR78
C	GLY104
C	LYS183
C	ARG256
D	GLY44
D	THR78
D	GLY104
D	LYS183
D	ARG256
A	GLY44
A	THR78
A	GLY104
A	LYS183
A	ARG256
B	GLY44
B	THR78
B	GLY104

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLY241
A	TYR258
B	GLY241
B	TYR258
C	GLY241
C	TYR258
D	GLY241
D	TYR258

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Important for dimerization => ECO:0000250

Chain	Residue	Details
A	PHE156
B	PHE156
C	PHE156
D	PHE156

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q15019

Chain	Residue	Details
A	LYS190
B	LYS190
C	LYS190
D	LYS190

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q15019

Chain	Residue	Details
A	TYR211
B	TYR211
C	TYR211
D	TYR211

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	SER218
B	SER218
C	SER218
D	SER218

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