6G60
Choline sulfatase from Ensifer (Sinorhizobium) meliloti cocrystalized with choline
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0008484 | molecular_function | sulfuric ester hydrolase activity |
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 | 0005737 | cellular_component | cytoplasm |
B | 0008484 | molecular_function | sulfuric ester hydrolase activity |
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 | 0005737 | cellular_component | cytoplasm |
C | 0008484 | molecular_function | sulfuric ester hydrolase activity |
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 | 0005737 | cellular_component | cytoplasm |
D | 0008484 | molecular_function | sulfuric ester hydrolase activity |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue CHT A 601 |
Chain | Residue |
A | ASN75 |
A | TYR123 |
A | TRP129 |
A | TRP143 |
A | HIS145 |
A | GLU386 |
A | LEU499 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue MG A 602 |
Chain | Residue |
A | ASP296 |
A | HIS297 |
A | ASP14 |
A | DDZ54 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 603 |
Chain | Residue |
A | ARG445 |
A | TRP449 |
A | MET451 |
A | GLU452 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 604 |
Chain | Residue |
A | HIS333 |
A | LEU334 |
A | THR335 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue CHT B 601 |
Chain | Residue |
B | ASN75 |
B | TYR123 |
B | TRP129 |
B | TRP143 |
B | HIS145 |
B | HIS201 |
B | GLU386 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue MG B 602 |
Chain | Residue |
B | ASP14 |
B | DDZ54 |
B | ASP296 |
B | HIS297 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 603 |
Chain | Residue |
B | HIS333 |
B | LEU334 |
B | THR335 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 604 |
Chain | Residue |
B | ARG71 |
B | HOH703 |
B | HOH739 |
D | ARG71 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 605 |
Chain | Residue |
B | GLN435 |
B | GLN435 |
B | LEU438 |
B | LEU438 |
B | ARG442 |
B | ARG442 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 606 |
Chain | Residue |
B | GLU182 |
B | ARG189 |
B | HOH844 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue CHT C 601 |
Chain | Residue |
C | ASN75 |
C | TYR123 |
C | TRP129 |
C | TRP143 |
C | HIS145 |
C | HIS201 |
C | GLU386 |
C | LEU499 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue MG C 602 |
Chain | Residue |
C | ASP14 |
C | DDZ54 |
C | ASP296 |
C | HIS297 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 603 |
Chain | Residue |
A | ARG71 |
C | ARG71 |
C | HOH713 |
C | HOH728 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue CHT D 1000 |
Chain | Residue |
D | DDZ54 |
D | ASN75 |
D | TYR123 |
D | TRP129 |
D | TRP143 |
D | HIS145 |
D | HIS201 |
D | LYS309 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue MG D 1001 |
Chain | Residue |
D | ASP14 |
D | DDZ54 |
D | LYS102 |
D | ASP296 |
D | HIS297 |
site_id | AD7 |
Number of Residues | 15 |
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 | ALA385 |
B | MG602 |
B | HOH760 |
site_id | AD8 |
Number of Residues | 14 |
Details | binding site for Di-peptide DDZ B 54 and ALA B 55 |
Chain | Residue |
B | HIS297 |
B | MG602 |
B | HOH760 |
B | HOH850 |
B | ASP14 |
B | LEU53 |
B | PRO56 |
B | ALA57 |
B | ARG58 |
B | ALA59 |
B | ASN75 |
B | LYS102 |
B | HIS104 |
B | ASP296 |
site_id | AD9 |
Number of Residues | 14 |
Details | binding site for Di-peptide LEU C 53 and DDZ C 54 |
Chain | Residue |
C | SER51 |
C | PRO52 |
C | ALA55 |
C | PRO56 |
C | ALA57 |
C | ARG58 |
C | ASN75 |
C | LYS102 |
C | HIS104 |
C | ASP296 |
C | HIS297 |
C | ALA385 |
C | MG602 |
C | HOH808 |
site_id | AE1 |
Number of Residues | 14 |
Details | binding site for Di-peptide DDZ C 54 and ALA C 55 |
Chain | Residue |
C | LEU53 |
C | PRO56 |
C | ALA57 |
C | ARG58 |
C | ALA59 |
C | ASP74 |
C | ASN75 |
C | LYS102 |
C | HIS104 |
C | ASP296 |
C | HIS297 |
C | MG602 |
C | HOH808 |
C | HOH886 |
site_id | AE2 |
Number of Residues | 13 |
Details | binding site for Di-peptide LEU D 53 and DDZ D 54 |
Chain | Residue |
D | SER51 |
D | PRO52 |
D | ALA55 |
D | PRO56 |
D | ALA57 |
D | ARG58 |
D | ASN75 |
D | LYS102 |
D | HIS104 |
D | HIS297 |
D | ALA385 |
D | CHT1000 |
D | MG1001 |
site_id | AE3 |
Number of Residues | 12 |
Details | binding site for Di-peptide DDZ D 54 and ALA D 55 |
Chain | Residue |
D | LEU53 |
D | PRO56 |
D | ALA57 |
D | ARG58 |
D | ALA59 |
D | ASN75 |
D | LYS102 |
D | HIS104 |
D | HIS297 |
D | CHT1000 |
D | MG1001 |
D | HOH1215 |
Functional Information from PROSITE/UniProt
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 | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P15289 |
Chain | Residue | Details |
A | DDZ54 | |
B | DDZ54 | |
C | DDZ54 | |
D | DDZ54 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P15289 |
Chain | Residue | Details |
A | HIS104 | |
B | HIS104 | |
C | HIS104 | |
D | HIS104 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP14 | |
C | GLN15 | |
C | ASP296 | |
C | HIS297 | |
D | ASP14 | |
D | GLN15 | |
D | ASP296 | |
D | HIS297 | |
A | GLN15 | |
A | ASP296 | |
A | HIS297 | |
B | ASP14 | |
B | GLN15 | |
B | ASP296 | |
B | HIS297 | |
C | ASP14 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: via 3-oxoalanine => ECO:0000250 |
Chain | Residue | Details |
A | DDZ54 | |
B | DDZ54 | |
C | DDZ54 | |
D | DDZ54 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: 3-oxoalanine (Cys) => ECO:0000250|UniProtKB:P15289 |
Chain | Residue | Details |
A | DDZ54 | |
B | DDZ54 | |
C | DDZ54 | |
D | DDZ54 |