1E33

Crystal structure of an Arylsulfatase A mutant P426L

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0004065	molecular_function	arylsulfatase activity
P	0004098	molecular_function	cerebroside-sulfatase activity
P	0005509	molecular_function	calcium ion binding
P	0005515	molecular_function	protein binding
P	0005576	cellular_component	extracellular region
P	0005764	cellular_component	lysosome
P	0005783	cellular_component	endoplasmic reticulum
P	0005788	cellular_component	endoplasmic reticulum lumen
P	0006629	biological_process	lipid metabolic process
P	0008484	molecular_function	sulfuric ester hydrolase activity
P	0016787	molecular_function	hydrolase activity
P	0035578	cellular_component	azurophil granule lumen
P	0043202	cellular_component	lysosomal lumen
P	0046872	molecular_function	metal ion binding
P	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

site_id	PS00149
Number of Residues	11
Details	SULFATASE_2 Sulfatases signature 2. GYlTgmAGK.WH

Chain	Residue	Details
P	GLY115-HIS125

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:7628016

Chain	Residue	Details
P	DDZ69

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:12888274

Chain	Residue	Details
P	HIS125

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K

Chain	Residue	Details
P	ASP29
P	ASP30
P	ASP281
P	ASN282

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: via 3-oxoalanine => ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K

Chain	Residue	Details
P	DDZ69

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11124905

Chain	Residue	Details
P	LYS123
P	SER150
P	HIS229
P	LYS302

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: 3-oxoalanine (Cys) => ECO:0000269|PubMed:7628016, ECO:0000269|PubMed:9342345

Chain	Residue	Details
P	DDZ69

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12888274, ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1N2K

Chain	Residue	Details
P	ASN158

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12888274, ECO:0007744|PDB:1N2K

Chain	Residue	Details
P	ASN184

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218

Chain	Residue	Details
P	ASN350

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	11
Details	M-CSA 158

Chain	Residue	Details
P	ASP29	metal ligand
P	ASP30	metal ligand
P	DDZ69	electrofuge, electrophile, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleophile, proton acceptor, proton donor, proton relay
P	ARG73	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
P	LYS123	electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
P	HIS125	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
P	SER150	electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
P	HIS229	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
P	ASP281	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
P	ASN282	metal ligand
P	LYS302	electrostatic stabiliser, hydrogen bond donor

---