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	ACT_SITE: Nucleophile => ECO:0000269|PubMed:24816101

Chain	Residue	Details
A	FGP70
B	FGP70

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV

Chain	Residue	Details
A	ASP31
A	ASP32
A	ASP273
A	ASN274
B	ASP31
B	ASP32
B	ASP273
B	ASN274

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: via 3-oxoalanine => ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV

Chain	Residue	Details
A	FGP70
B	FGP70

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: 3-oxoalanine (Cys) => ECO:0000269|PubMed:24816101

Chain	Residue	Details
A	FGP70
B	FGP70

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site_id	SWS_FT_FI5
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV

Chain	Residue	Details
A	ASN41
B	ASN41

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site_id	SWS_FT_FI6
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN142
B	ASN142

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site_id	SWS_FT_FI7
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV

Chain	Residue	Details
A	ASN151
B	ASN151

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site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV

Chain	Residue	Details
A	ASN264
B	ASN264

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site_id	SWS_FT_FI9
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV

Chain	Residue	Details
A	ASN413
B	ASN413

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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	ARG74	electrostatic stabiliser
A	LYS123	electrostatic stabiliser
A	HIS125	electrostatic stabiliser, proton acceptor, proton donor
A	HIS181	proton acceptor, proton donor
A	ASP273	metal ligand, proton acceptor, proton donor
A	ASN274	metal ligand
A	ARG282	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	ARG74	electrostatic stabiliser
B	LYS123	electrostatic stabiliser
B	HIS125	electrostatic stabiliser, proton acceptor, proton donor
B	HIS181	proton acceptor, proton donor
B	ASP273	metal ligand, proton acceptor, proton donor
B	ASN274	metal ligand
B	ARG282	electrostatic stabiliser

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