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

Chain	Residue	Details
A	FGP70
B	FGP70
C	FGP70
D	FGP70
E	FGP70
F	FGP70
G	FGP70
H	FGP70

site_id	SWS_FT_FI2
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269\|PubMed:24816101, ECO:0007744\|PDB:4MHX, ECO:0007744\|PDB:4MIV

Chain	Residue	Details
A	ASP31
C	ASP32
C	ASP273
C	ASN274
D	ASP31
D	ASP32
D	ASP273
D	ASN274
E	ASP31
E	ASP32
E	ASP273
A	ASP32
E	ASN274
F	ASP31
F	ASP32
F	ASP273
F	ASN274
G	ASP31
G	ASP32
G	ASP273
G	ASN274
H	ASP31
A	ASP273
H	ASP32
H	ASP273
H	ASN274
A	ASN274
B	ASP31
B	ASP32
B	ASP273
B	ASN274
C	ASP31

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: via 3-oxoalanine => ECO:0000269\|PubMed:24816101, ECO:0007744\|PDB:4MHX, ECO:0007744\|PDB:4MIV

Chain	Residue	Details
A	FGP70
B	FGP70
C	FGP70
D	FGP70
E	FGP70
F	FGP70
G	FGP70
H	FGP70

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: 3-oxoalanine (Cys) => ECO:0000269\|PubMed:24816101

Chain	Residue	Details
A	FGP70
B	FGP70
C	FGP70
D	FGP70
E	FGP70
F	FGP70
G	FGP70
H	FGP70

site_id	SWS_FT_FI5
Number of Residues	8
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
C	ASN41
D	ASN41
E	ASN41
F	ASN41
G	ASN41
H	ASN41

site_id	SWS_FT_FI6
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN142
B	ASN142
C	ASN142
D	ASN142
E	ASN142
F	ASN142
G	ASN142
H	ASN142

site_id	SWS_FT_FI7
Number of Residues	8
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
C	ASN151
D	ASN151
E	ASN151
F	ASN151
G	ASN151
H	ASN151

site_id	SWS_FT_FI8
Number of Residues	8
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
C	ASN264
D	ASN264
E	ASN264
F	ASN264
G	ASN264
H	ASN264

site_id	SWS_FT_FI9
Number of Residues	8
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
C	ASN413
D	ASN413
E	ASN413
F	ASN413
G	ASN413
H	ASN413

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

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

site_id	MCSA3
Number of Residues	9
Details	M-CSA 951

Chain	Residue	Details
C	ASP31	metal ligand
C	ASP32	metal ligand
C	ARG74	electrostatic stabiliser
C	LYS123	electrostatic stabiliser
C	HIS125	electrostatic stabiliser, proton acceptor, proton donor
C	HIS181	proton acceptor, proton donor
C	ASP273	metal ligand, proton acceptor, proton donor
C	ASN274	metal ligand
C	ARG282	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	ARG74	electrostatic stabiliser
D	LYS123	electrostatic stabiliser
D	HIS125	electrostatic stabiliser, proton acceptor, proton donor
D	HIS181	proton acceptor, proton donor
D	ASP273	metal ligand, proton acceptor, proton donor
D	ASN274	metal ligand
D	ARG282	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	ARG74	electrostatic stabiliser
E	LYS123	electrostatic stabiliser
E	HIS125	electrostatic stabiliser, proton acceptor, proton donor
E	HIS181	proton acceptor, proton donor
E	ASP273	metal ligand, proton acceptor, proton donor
E	ASN274	metal ligand
E	ARG282	electrostatic stabiliser

site_id	MCSA6
Number of Residues	9
Details	M-CSA 951

Chain	Residue	Details
F	ASP31	metal ligand
F	ASP32	metal ligand
F	ARG74	electrostatic stabiliser
F	LYS123	electrostatic stabiliser
F	HIS125	electrostatic stabiliser, proton acceptor, proton donor
F	HIS181	proton acceptor, proton donor
F	ASP273	metal ligand, proton acceptor, proton donor
F	ASN274	metal ligand
F	ARG282	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	ARG74	electrostatic stabiliser
G	LYS123	electrostatic stabiliser
G	HIS125	electrostatic stabiliser, proton acceptor, proton donor
G	HIS181	proton acceptor, proton donor
G	ASP273	metal ligand, proton acceptor, proton donor
G	ASN274	metal ligand
G	ARG282	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	ARG74	electrostatic stabiliser
H	LYS123	electrostatic stabiliser
H	HIS125	electrostatic stabiliser, proton acceptor, proton donor
H	HIS181	proton acceptor, proton donor
H	ASP273	metal ligand, proton acceptor, proton donor
H	ASN274	metal ligand
H	ARG282	electrostatic stabiliser

219140

PDB entries from 2024-05-01

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