Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4MIV

Crystal Structure of Sulfamidase, Crystal Form L

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
C	0003824	molecular_function	catalytic activity
C	0008484	molecular_function	sulfuric ester hydrolase activity
D	0003824	molecular_function	catalytic activity
D	0008484	molecular_function	sulfuric ester hydrolase activity
E	0003824	molecular_function	catalytic activity
E	0008484	molecular_function	sulfuric ester hydrolase activity
F	0003824	molecular_function	catalytic activity
F	0008484	molecular_function	sulfuric ester hydrolase activity
G	0003824	molecular_function	catalytic activity
G	0008484	molecular_function	sulfuric ester hydrolase activity
H	0003824	molecular_function	catalytic activity
H	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

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

Chain	Residue	Details
A	SER68-GLY80

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24816101","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	32
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

site_id	SWS_FT_FI3
Number of Residues	8
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

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"3-oxoalanine (Cys)","evidences":[{"source":"PubMed","id":"24816101","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
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

site_id	SWS_FT_FI6
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
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

site_id	SWS_FT_FI8
Number of Residues	8
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

site_id	SWS_FT_FI9
Number of Residues	8
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

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

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

site_id	MCSA3
Number of Residues	9
Details	M-CSA 951

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

site_id	MCSA4
Number of Residues	9
Details	M-CSA 951

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

site_id	MCSA5
Number of Residues	9
Details	M-CSA 951

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

site_id	MCSA6
Number of Residues	8
Details	M-CSA 951

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

site_id	MCSA7
Number of Residues	9
Details	M-CSA 951

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

site_id	MCSA8
Number of Residues	9
Details	M-CSA 951

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)