4MHX

Crystal Structure of Sulfamidase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0008484	molecular_function	sulfuric ester hydrolase activity
B	0003824	molecular_function	catalytic activity
B	0008484	molecular_function	sulfuric ester hydrolase activity

Functional Information from PROSITE/UniProt

site_id	PS00149
Number of Residues	11
Details	SULFATASE_2 Sulfatases signature 2. GVrTgiIGK.KH

Chain	Residue	Details
A	GLY115-HIS125

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site_id	PS00523
Number of Residues	13
Details	SULFATASE_1 Sulfatases signature 1. SSSSPSRasLLTG

Chain	Residue	Details
A	SER68-GLY80

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24816101","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24816101","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MIV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"description":"via 3-oxoalanine","evidences":[{"source":"PubMed","id":"24816101","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MIV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"3-oxoalanine (Cys)","evidences":[{"source":"PubMed","id":"24816101","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24816101","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MIV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"24816101","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MIV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24816101","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MIV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24816101","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MIV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 951

Chain	Residue	Details
A	ASP31	metal ligand
A	ASP32	metal ligand
A	LEU78	electrostatic stabiliser
A	GLY127	electrostatic stabiliser
A	GLU129	electrostatic stabiliser, proton acceptor, proton donor
A	HIS185	proton acceptor, proton donor
A	PRO277	metal ligand, proton acceptor, proton donor
A	PHE278	metal ligand
A	TYR286	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	9
Details	M-CSA 951

Chain	Residue	Details
B	ASP31	metal ligand
B	ASP32	metal ligand
B	LEU78	electrostatic stabiliser
B	GLY127	electrostatic stabiliser
B	GLU129	electrostatic stabiliser, proton acceptor, proton donor
B	HIS185	proton acceptor, proton donor
B	PRO277	metal ligand, proton acceptor, proton donor
B	PHE278	metal ligand
B	TYR286	electrostatic stabiliser

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