2SNS

STAPHYLOCOCCAL NUCLEASE. PROPOSED MECHANISM OF ACTION BASED ON STRUCTURE OF ENZYME-THYMIDINE 3(PRIME),5(PRIME)-BIPHOSPHATE-CALCIUM ION COMPLEX AT 1.5-ANGSTROMS RESOLUTION

Replaces:  1SNS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0004518	molecular_function	nuclease activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 150

Chain	Residue
A	ASP40
A	THR41
A	THP151
A	ASP21
A	ARG35

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site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE THP A 151

Chain	Residue
A	ASP21
A	ARG35
A	LEU37
A	ASP40
A	LYS71
A	TYR85
A	ARG87
A	LEU89
A	TYR115
A	CA150

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site_id	CAB
Number of Residues	4
Details	IDENTIFIES THE FOUR RESIDUES WHICH SUPPLY OXYGEN ATOMS TO BIND THE CALCIUM ION

Chain	Residue
A	ASP21
A	ASP40
A	THR41
A	THP151

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site_id	PO4
Number of Residues	3
Details	RESIDUES WHICH BIND THE INHIBITOR MOLECULE

Chain	Residue
A	ARG35
A	ARG87
A	TYR85

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Functional Information from PROSITE/UniProt

site_id	PS01123
Number of Residues	25
Details	TNASE_1 Thermonuclease family signature 1. DGDTVkLmykgqpmtf.RLllVDtPE

Chain	Residue	Details
A	ASP19-GLU43

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site_id	PS01284
Number of Residues	11
Details	TNASE_2 Thermonuclease family signature 2. DKYGRgLAyIY

Chain	Residue	Details
A	ASP83-TYR93

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:288045

Chain	Residue	Details
A	ARG35
A	GLU43
A	ARG87

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING:

Chain	Residue	Details
A	ASP21
A	ASP40
A	THR41

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 165

Chain	Residue	Details
A	ASP21	metal ligand
A	ARG35	electrostatic stabiliser, hydrogen bond donor
A	ASP40	metal ligand
A	THR41	metal ligand
A	GLU43	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ARG87	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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