5DSF

Crystal structure of the mercury-bound form of MerB mutant D99S

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016829	molecular_function	lyase activity
A	0018836	molecular_function	alkylmercury lyase activity
A	0046413	biological_process	obsolete obsolete organomercury catabolic process
A	0046689	biological_process	response to mercury ion
B	0016829	molecular_function	lyase activity
B	0018836	molecular_function	alkylmercury lyase activity
B	0046413	biological_process	obsolete obsolete organomercury catabolic process
B	0046689	biological_process	response to mercury ion

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue HG A 301

Chain	Residue
A	CYS96
A	SER99
A	CYS159
A	HOH488

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site_id	AC2
Number of Residues	2
Details	binding site for residue BR A 302

Chain	Residue
A	LYS2
B	PRO5

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site_id	AC3
Number of Residues	5
Details	binding site for residue HG B 301

Chain	Residue
B	HOH486
B	HOH495
B	CYS96
B	SER99
B	CYS159

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 297

Chain	Residue	Details
A	CYS96	activator, covalently attached, hydrogen bond donor, nucleophile, proton donor
A	SER99	activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
A	CYS159	activator, covalently attached, nucleophile, proton donor

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site_id	MCSA2
Number of Residues	3
Details	M-CSA 297

Chain	Residue	Details
B	CYS96	activator, covalently attached, hydrogen bond donor, nucleophile, proton donor
B	SER99	activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
B	CYS159	activator, covalently attached, nucleophile, proton donor

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