Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FNY

CRYSTAL STRUCTURE OF A CHOLINE SULFATASE FROM SINORHIZOBIUM MELLILOTI

Replaces: 4UG4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004423	molecular_function	iduronate-2-sulfatase activity
A	0005737	cellular_component	cytoplasm
A	0016787	molecular_function	hydrolase activity
A	0042425	biological_process	choline biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0047753	molecular_function	choline-sulfatase activity
B	0004423	molecular_function	iduronate-2-sulfatase activity
B	0005737	cellular_component	cytoplasm
B	0016787	molecular_function	hydrolase activity
B	0042425	biological_process	choline biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0047753	molecular_function	choline-sulfatase activity
C	0004423	molecular_function	iduronate-2-sulfatase activity
C	0005737	cellular_component	cytoplasm
C	0016787	molecular_function	hydrolase activity
C	0042425	biological_process	choline biosynthetic process
C	0046872	molecular_function	metal ion binding
C	0047753	molecular_function	choline-sulfatase activity
D	0004423	molecular_function	iduronate-2-sulfatase activity
D	0005737	cellular_component	cytoplasm
D	0016787	molecular_function	hydrolase activity
D	0042425	biological_process	choline biosynthetic process
D	0046872	molecular_function	metal ion binding
D	0047753	molecular_function	choline-sulfatase activity
E	0004423	molecular_function	iduronate-2-sulfatase activity
E	0005737	cellular_component	cytoplasm
E	0016787	molecular_function	hydrolase activity
E	0042425	biological_process	choline biosynthetic process
E	0046872	molecular_function	metal ion binding
E	0047753	molecular_function	choline-sulfatase activity
F	0004423	molecular_function	iduronate-2-sulfatase activity
F	0005737	cellular_component	cytoplasm
F	0016787	molecular_function	hydrolase activity
F	0042425	biological_process	choline biosynthetic process
F	0046872	molecular_function	metal ion binding
F	0047753	molecular_function	choline-sulfatase activity
G	0004423	molecular_function	iduronate-2-sulfatase activity
G	0005737	cellular_component	cytoplasm
G	0016787	molecular_function	hydrolase activity
G	0042425	biological_process	choline biosynthetic process
G	0046872	molecular_function	metal ion binding
G	0047753	molecular_function	choline-sulfatase activity
H	0004423	molecular_function	iduronate-2-sulfatase activity
H	0005737	cellular_component	cytoplasm
H	0016787	molecular_function	hydrolase activity
H	0042425	biological_process	choline biosynthetic process
H	0046872	molecular_function	metal ion binding
H	0047753	molecular_function	choline-sulfatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 601

Chain	Residue
A	ASP14
A	LEU53
A	DDZ54
A	CYS54
A	ASP296
A	HIS297

site_id	AC2
Number of Residues	6
Details	binding site for residue CA B 601

Chain	Residue
B	CYS54
B	ASP296
B	HIS297
B	ASP14
B	LEU53
B	DDZ54

site_id	AC3
Number of Residues	5
Details	binding site for residue CA C 601

Chain	Residue
C	ASP14
C	CYS54
C	DDZ54
C	ASP296
C	HIS297

site_id	AC4
Number of Residues	6
Details	binding site for residue CA D 601

Chain	Residue
D	ASP14
D	LEU53
D	DDZ54
D	CYS54
D	ASP296
D	HIS297

site_id	AC5
Number of Residues	6
Details	binding site for residue CA E 601

Chain	Residue
E	ASP14
E	LEU53
E	DDZ54
E	CYS54
E	ASP296
E	HIS297

site_id	AC6
Number of Residues	6
Details	binding site for residue CA F 601

Chain	Residue
F	ASP14
F	LEU53
F	DDZ54
F	CYS54
F	ASP296
F	HIS297

site_id	AC7
Number of Residues	5
Details	binding site for residue CA G 601

Chain	Residue
G	ASP14
G	DDZ54
G	CYS54
G	ASP296
G	HIS297

site_id	AC8
Number of Residues	5
Details	binding site for residue CA H 601

Chain	Residue
H	ASP14
H	DDZ54
H	CYS54
H	ASP296
H	HIS297

site_id	AC9
Number of Residues	16
Details	binding site for Di-peptide LEU B 53 and DDZ B 54

Chain	Residue
B	ASP14
B	SER51
B	PRO52
B	ALA55
B	PRO56
B	ALA57
B	ARG58
B	ASN75
B	LYS102
B	HIS104
B	ASP296
B	HIS297
B	LYS309
B	GLU386
B	CA601
B	HOH897

site_id	AD1
Number of Residues	14
Details	binding site for Di-peptide DDZ B 54 and ALA B 55

Chain	Residue
B	ASP14
B	LEU53
B	PRO56
B	ALA57
B	ARG58
B	ALA59
B	ASP74
B	ASN75
B	LYS102
B	HIS104
B	ASP296
B	HIS297
B	CA601
B	HOH897

site_id	AD2
Number of Residues	15
Details	binding site for Di-peptide LEU C 53 and DDZ C 54

Chain	Residue
C	ASP14
C	SER51
C	PRO52
C	ALA55
C	PRO56
C	ALA57
C	ARG58
C	ASN75
C	LYS102
C	HIS104
C	HIS297
C	ALA385
C	GLU386
C	CA601
C	HOH863

site_id	AD3
Number of Residues	13
Details	binding site for Di-peptide DDZ C 54 and ALA C 55

Chain	Residue
C	HIS104
C	HIS297
C	CA601
C	HOH863
C	ASP14
C	LEU53
C	PRO56
C	ALA57
C	ARG58
C	ALA59
C	ASP74
C	ASN75
C	LYS102

site_id	AD4
Number of Residues	16
Details	binding site for Di-peptide LEU D 53 and DDZ D 54

Chain	Residue
D	ASP14
D	SER51
D	PRO52
D	ALA55
D	PRO56
D	ALA57
D	ARG58
D	ASN75
D	LYS102
D	HIS104
D	ASP296
D	HIS297
D	ALA385
D	GLU386
D	CA601
D	HOH863

site_id	AD5
Number of Residues	14
Details	binding site for Di-peptide DDZ D 54 and ALA D 55

Chain	Residue
D	ASP14
D	LEU53
D	PRO56
D	ALA57
D	ARG58
D	ALA59
D	ASP74
D	ASN75
D	LYS102
D	HIS104
D	ASP296
D	HIS297
D	CA601
D	HOH863

site_id	AD6
Number of Residues	14
Details	binding site for Di-peptide LEU E 53 and DDZ E 54

Chain	Residue
E	ASP14
E	SER51
E	PRO52
E	ALA55
E	PRO56
E	ALA57
E	ARG58
E	ASN75
E	LYS102
E	HIS104
E	ASP296
E	HIS297
E	CA601
E	HOH867

site_id	AD7
Number of Residues	13
Details	binding site for Di-peptide DDZ E 54 and ALA E 55

Chain	Residue
E	ASP14
E	LEU53
E	PRO56
E	ALA57
E	ARG58
E	ALA59
E	ASP74
E	ASN75
E	LYS102
E	HIS104
E	CA601
E	HOH841
E	HOH867

site_id	AD8
Number of Residues	14
Details	binding site for Di-peptide LEU F 53 and DDZ F 54

Chain	Residue
F	ASP14
F	SER51
F	PRO52
F	ALA55
F	PRO56
F	ALA57
F	ARG58
F	ASN75
F	LYS102
F	HIS104
F	ASP296
F	HIS297
F	GLU386
F	CA601

site_id	AD9
Number of Residues	13
Details	binding site for Di-peptide DDZ F 54 and ALA F 55

Chain	Residue
F	ASP14
F	LEU53
F	PRO56
F	ALA57
F	ARG58
F	ALA59
F	ASP74
F	ASN75
F	LYS102
F	HIS104
F	ASP296
F	HIS297
F	CA601

site_id	AE1
Number of Residues	16
Details	binding site for Di-peptide LEU G 53 and DDZ G 54

Chain	Residue
G	ASP14
G	SER51
G	PRO52
G	ALA55
G	PRO56
G	ALA57
G	ARG58
G	ASN75
G	LYS102
G	HIS104
G	HIS297
G	LYS309
G	ALA385
G	GLU386
G	CA601
G	HOH803

site_id	AE2
Number of Residues	12
Details	binding site for Di-peptide DDZ G 54 and ALA G 55

Chain	Residue
G	ASP14
G	LEU53
G	PRO56
G	ALA57
G	ARG58
G	ALA59
G	ASN75
G	LYS102
G	HIS104
G	HIS297
G	CA601
G	HOH803

site_id	AE3
Number of Residues	17
Details	binding site for Di-peptide LEU H 53 and DDZ H 54

Chain	Residue
H	ASP14
H	SER51
H	PRO52
H	ALA55
H	PRO56
H	ALA57
H	ARG58
H	ASN75
H	LYS102
H	HIS104
H	ASP296
H	HIS297
H	LYS309
H	ALA385
H	GLU386
H	CA601
H	HOH841

site_id	AE4
Number of Residues	15
Details	binding site for Di-peptide DDZ H 54 and ALA H 55

Chain	Residue
H	ASP14
H	LEU53
H	PRO56
H	ALA57
H	ARG58
H	ALA59
H	ASN75
H	LYS102
H	HIS104
H	ASP296
H	HIS297
H	LYS309
H	CA601
H	HOH807
H	HOH841

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO52-GLY64

site_id	PS00149
Number of Residues	11
Details	SULFATASE_2 Sulfatases signature 2. GYyTalSGK.MH

Chain	Residue	Details
A	GLY94-HIS104

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Nucleophile => ECO:0000250\|UniProtKB:P15289

Chain	Residue	Details
A	CYS54
B	CYS54
C	CYS54
D	CYS54
E	CYS54
F	CYS54
G	CYS54
H	CYS54

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000250\|UniProtKB:P15289

Chain	Residue	Details
A	HIS104
B	HIS104
C	HIS104
D	HIS104
E	HIS104
F	HIS104
G	HIS104
H	HIS104

site_id	SWS_FT_FI3
Number of Residues	32
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASP14
C	GLN15
C	ASP296
C	HIS297
D	ASP14
D	GLN15
D	ASP296
D	HIS297
E	ASP14
E	GLN15
E	ASP296
A	GLN15
E	HIS297
F	ASP14
F	GLN15
F	ASP296
F	HIS297
G	ASP14
G	GLN15
G	ASP296
G	HIS297
H	ASP14
A	ASP296
H	GLN15
H	ASP296
H	HIS297
A	HIS297
B	ASP14
B	GLN15
B	ASP296
B	HIS297
C	ASP14

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: via 3-oxoalanine => ECO:0000250

Chain	Residue	Details
A	CYS54
B	CYS54
C	CYS54
D	CYS54
E	CYS54
F	CYS54
G	CYS54
H	CYS54

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: 3-oxoalanine (Cys) => ECO:0000250\|UniProtKB:P15289

Chain	Residue	Details
A	CYS54
B	CYS54
C	CYS54
D	CYS54
E	CYS54
F	CYS54
G	CYS54
H	CYS54

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