1AVQ

TOROIDAL STRUCTURE OF LAMBDA EXONUCLEASE DETERMINED AT 2.4 ANGSTROMS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004518	molecular_function	nuclease activity
A	0004527	molecular_function	exonuclease activity
A	0006259	biological_process	DNA metabolic process
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0051908	molecular_function	double-stranded DNA 5'-3' DNA exonuclease activity
B	0004518	molecular_function	nuclease activity
B	0004527	molecular_function	exonuclease activity
B	0006259	biological_process	DNA metabolic process
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0051908	molecular_function	double-stranded DNA 5'-3' DNA exonuclease activity
C	0004518	molecular_function	nuclease activity
C	0004527	molecular_function	exonuclease activity
C	0006259	biological_process	DNA metabolic process
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
C	0051908	molecular_function	double-stranded DNA 5'-3' DNA exonuclease activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 227

Chain	Residue
A	ARG28
A	THR33
A	ALA34
A	SER35
A	CYS116
A	SER117
A	GLN157
A	HOH267

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site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 B 227

Chain	Residue
B	THR33
B	ALA34
B	SER35
B	CYS116
B	SER117
B	GLN157
B	HOH309
B	ARG28

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site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 227

Chain	Residue
C	ARG28
C	THR33
C	ALA34
C	SER35
C	CYS116
C	SER117
C	HOH247

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site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACT A 228

Chain	Residue
A	SER198

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site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ACT B 228

Chain	Residue
B	SER198

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site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT C 228

Chain	Residue
C	LYS194
C	TYR195
C	SER198

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site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT C 229

Chain	Residue
C	THR2
C	ILE5
C	ILE6
C	ASP109
C	GLU110
C	HOH237
C	HOH278

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 10508668

Chain	Residue	Details
A	LYS131

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site_id	CSA2
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 10508668

Chain	Residue	Details
B	LYS131

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site_id	CSA3
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 10508668

Chain	Residue	Details
C	LYS131

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site_id	MCSA1
Number of Residues	6
Details	M-CSA 836

Chain	Residue	Details
A	GLU93	metal ligand
A	GLU102	electrostatic stabiliser
A	ASP109	metal ligand
A	GLU129	increase nucleophilicity, metal ligand, proton acceptor, proton donor
A	LEU130	metal ligand
A	LYS131	electrostatic stabiliser, proton acceptor, proton donor, proton relay

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site_id	MCSA2
Number of Residues	6
Details	M-CSA 836

Chain	Residue	Details
B	GLU93	metal ligand
B	GLU102	electrostatic stabiliser
B	ASP109	metal ligand
B	GLU129	increase nucleophilicity, metal ligand, proton acceptor, proton donor
B	LEU130	metal ligand
B	LYS131	electrostatic stabiliser, proton acceptor, proton donor, proton relay

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site_id	MCSA3
Number of Residues	6
Details	M-CSA 836

Chain	Residue	Details
C	GLU93	metal ligand
C	GLU102	electrostatic stabiliser
C	ASP109	metal ligand
C	GLU129	increase nucleophilicity, metal ligand, proton acceptor, proton donor
C	LEU130	metal ligand
C	LYS131	electrostatic stabiliser, proton acceptor, proton donor, proton relay

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