2ZOD

Crystal structure of selenophosphate synthetase from Aquifex aeolicus

Replaces:  2YYD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004756	molecular_function	selenide, water dikinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0016260	biological_process	selenocysteine biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0004756	molecular_function	selenide, water dikinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0016260	biological_process	selenocysteine biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016310	biological_process	phosphorylation
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 701

Chain	Residue
A	LYS179
A	PRO263
A	LYS264

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 702

Chain	Residue
B	SER10
B	LYS179
B	PRO263
B	LYS264

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00625

Chain	Residue	Details
A	CYS13
B	CYS13

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00625

Chain	Residue	Details
A	LYS16
A	ILE41
A	ASP60
B	LYS16
B	ILE41
B	ASP60

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00625

Chain	Residue	Details
A	ASP44
A	ASP83
A	GLY131
A	ASP219
B	ASP44
B	ASP83
B	GLY131
B	ASP219

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00625

Chain	Residue	Details
A	LYS16
B	LYS16

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