1LJU

X-RAY STRUCTURE OF C15A ARSENATE REDUCTASE FROM PI258 COMPLEXED WITH ARSENITE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004725	molecular_function	protein tyrosine phosphatase activity
A	0005737	cellular_component	cytoplasm
A	0016491	molecular_function	oxidoreductase activity
A	0030612	molecular_function	arsenate reductase (thioredoxin) activity
A	0046685	biological_process	response to arsenic-containing substance
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 134

Chain	Residue
A	ASN13
A	GLU21
A	SER36
A	THR63
A	ASP65
A	HOH141

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000305|PubMed:11573087, ECO:0000305|PubMed:12072565

Chain	Residue	Details
A	CSR10
A	CYS82
A	CYS89

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11573087, ECO:0000269|PubMed:12072565, ECO:0000269|PubMed:12682056, ECO:0000269|PubMed:15159594, ECO:0000269|PubMed:16797027

Chain	Residue	Details
A	ASN13
A	SER36
A	THR63
A	ASP65

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	14
Details	M-CSA 143

Chain	Residue	Details
A	THR11	electrofuge, electrophile, nucleofuge, nucleophile
A	ILE67
A	ASN69
A	ASP86	electrofuge, electrophile, hydrogen bond acceptor, nucleofuge, nucleophile
A	PRO93	hydrogen bond acceptor, nucleofuge, nucleophile
A	LYS109	electrostatic stabiliser, hydrogen bond acceptor
A	ALA15	electrostatic stabiliser, hydrogen bond donor
A	ARG16	electrostatic stabiliser, hydrogen bond donor
A	SER17	electrostatic stabiliser, hydrogen bond donor
A	GLN18	electrostatic stabiliser, hydrogen bond donor
A	MET19	electrostatic stabiliser, hydrogen bond donor
A	ALA20	electrostatic stabiliser, hydrogen bond donor
A	GLU21	electrostatic stabiliser, hydrogen bond donor
A	GLU40

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