5AJ9
G7 mutant of PAS, arylsulfatase from Pseudomonas Aeruginosa
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004065 | molecular_function | arylsulfatase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008081 | molecular_function | phosphoric diester hydrolase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004065 | molecular_function | arylsulfatase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0008081 | molecular_function | phosphoric diester hydrolase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 1452 |
Chain | Residue |
B | ILE400 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 1529 |
Chain | Residue |
A | ASP13 |
A | ASP14 |
A | DDZ51 |
A | ASP317 |
A | ASN318 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1530 |
Chain | Residue |
A | HIS211 |
A | LYS375 |
A | DDZ51 |
A | LYS113 |
A | HIS115 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1531 |
Chain | Residue |
A | HIS452 |
A | THR456 |
A | HOH2202 |
A | HOH2203 |
B | ASN455 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 1532 |
Chain | Residue |
A | THR262 |
A | ARG263 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1533 |
Chain | Residue |
A | GLN506 |
A | PRO507 |
A | GLY508 |
A | LYS509 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1534 |
Chain | Residue |
A | VAL357 |
A | TRP358 |
A | HOH2155 |
A | HOH2164 |
A | HOH2172 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1535 |
Chain | Residue |
A | TYR143 |
A | PRO217 |
A | ARG218 |
A | GLU219 |
A | HOH2075 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 1536 |
Chain | Residue |
A | GLN197 |
A | GLN304 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MES A 1537 |
Chain | Residue |
A | ARG236 |
A | GLN237 |
A | GLU254 |
A | ALA255 |
B | ASP229 |
B | TRP265 |
B | ARG273 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 1538 |
Chain | Residue |
A | ARG242 |
site_id | BC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 1539 |
Chain | Residue |
A | ARG289 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1529 |
Chain | Residue |
B | ASP13 |
B | ASP14 |
B | DDZ51 |
B | ASP317 |
B | ASN318 |
B | SO41530 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 1530 |
Chain | Residue |
B | DDZ51 |
B | LYS113 |
B | HIS115 |
B | HIS211 |
B | LYS375 |
B | CA1529 |
B | HOH2200 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1531 |
Chain | Residue |
A | ASN455 |
B | HIS452 |
B | THR456 |
B | HOH2187 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1532 |
Chain | Residue |
B | GLN506 |
B | PRO507 |
B | GLY508 |
B | LYS509 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1533 |
Chain | Residue |
B | ASN345 |
B | VAL357 |
B | TRP358 |
B | HOH2161 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 1534 |
Chain | Residue |
B | TYR143 |
B | PRO217 |
B | ARG218 |
B | GLU219 |
B | HOH2071 |
site_id | CC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 1535 |
Chain | Residue |
B | THR262 |
B | ARG263 |
site_id | CC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MES B 1536 |
Chain | Residue |
A | ASP229 |
A | TRP265 |
A | ARG273 |
A | HOH2106 |
B | GLN237 |
B | VAL253 |
B | GLU254 |
B | ALA255 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 1537 |
Chain | Residue |
B | HIS89 |
B | LYS119 |
B | GLN122 |
site_id | CC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 1538 |
Chain | Residue |
B | PHE404 |
site_id | CC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 1539 |
Chain | Residue |
B | PRO333 |
B | ASP334 |
Functional Information from PROSITE/UniProt
site_id | PS00149 |
Number of Residues | 11 |
Details | SULFATASE_2 Sulfatases signature 2. GYqTlmAGK.WH |
Chain | Residue | Details |
A | GLY105-HIS115 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:11435113, ECO:0000269|PubMed:9748219 |
Chain | Residue | Details |
A | DDZ51 | |
B | DDZ51 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P15289 |
Chain | Residue | Details |
A | HIS115 | |
B | HIS115 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11435113 |
Chain | Residue | Details |
A | ASP13 | |
A | ASP14 | |
A | ASP317 | |
A | ASN318 | |
B | ASP13 | |
B | ASP14 | |
B | ASP317 | |
B | ASN318 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: via 3-oxoalanine => ECO:0000269|PubMed:11435113 |
Chain | Residue | Details |
A | DDZ51 | |
B | DDZ51 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: 3-oxoalanine (Cys) => ECO:0000269|PubMed:11435113, ECO:0000269|PubMed:9748219 |
Chain | Residue | Details |
A | DDZ51 | |
B | DDZ51 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 661 |
Chain | Residue | Details |
A | ASP13 | metal ligand |
A | LYS375 | electrostatic stabiliser |
A | ASP14 | metal ligand |
A | DDZ51 | covalently attached, increase electrophilicity, metal ligand, nucleophile, proton donor |
A | ARG55 | electrostatic stabiliser |
A | LYS113 | electrostatic stabiliser, increase electrophilicity |
A | HIS115 | electrostatic stabiliser, proton acceptor |
A | HIS211 | electrostatic stabiliser, proton donor |
A | ASP317 | activator, increase nucleophilicity, metal ligand, proton acceptor |
A | ASN318 | metal ligand |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 661 |
Chain | Residue | Details |
B | ASP13 | metal ligand |
B | LYS375 | electrostatic stabiliser |
B | ASP14 | metal ligand |
B | DDZ51 | covalently attached, increase electrophilicity, metal ligand, nucleophile, proton donor |
B | ARG55 | electrostatic stabiliser |
B | LYS113 | electrostatic stabiliser, increase electrophilicity |
B | HIS115 | electrostatic stabiliser, proton acceptor |
B | HIS211 | electrostatic stabiliser, proton donor |
B | ASP317 | activator, increase nucleophilicity, metal ligand, proton acceptor |
B | ASN318 | metal ligand |