5XD9

Crystal structure analysis of 3,6-anhydro-L-galactonate cycloisomerase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016836	molecular_function	hydro-lyase activity
A	0016853	molecular_function	isomerase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 401

Chain	Residue
A	ASP198
A	ASN200
A	GLU224
A	GLU225
A	GLU250

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site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 402

Chain	Residue
A	ASN300
A	TYR52
A	TYR94
A	GLU250
A	ASP273

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q8ZL58

Chain	Residue	Details
A	LYS169

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q8ZL58

Chain	Residue	Details
A	ASN300

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q8ZL58

Chain	Residue	Details
A	ASP198
A	GLU224
A	GLU250

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 946

Chain	Residue	Details
A	LYS169	proton shuttle (general acid/base)
A	ASP198	metal ligand
A	GLU224	metal ligand
A	GLU250	metal ligand
A	ASP273	modifies pKa
A	ASN300	proton shuttle (general acid/base)

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