5XD7

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0016052	biological_process	carbohydrate catabolic process
A	0016836	molecular_function	hydro-lyase activity
A	0016853	molecular_function	isomerase activity
A	0019388	biological_process	galactose catabolic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue MG A 402

Chain	Residue
A	LYS167
A	ASP198
A	GLU224
A	GLU250
A	ACY403
A	HOH508
A	HOH586

---

site_id	AC2
Number of Residues	6
Details	binding site for residue ACY A 403

Chain	Residue
A	GLU250
A	HIS300
A	HIS321
A	MG402
A	LYS169
A	ASN200

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q8ZL58","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q8ZL58","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8ZL58","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

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	HIS300	proton shuttle (general acid/base)

---