1HDH
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 | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1528 |
Chain | Residue |
A | ASP13 |
A | ASP14 |
A | DDZ51 |
A | ASP317 |
A | ASN318 |
A | SO41529 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 A 1529 |
Chain | Residue |
A | DDZ51 |
A | MET72 |
A | LYS113 |
A | HIS115 |
A | GLY138 |
A | HIS211 |
A | LYS375 |
A | CA1528 |
A | ASP13 |
A | ASP14 |
A | THR50 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 1530 |
Chain | Residue |
A | THR262 |
A | ARG263 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1531 |
Chain | Residue |
A | ARG438 |
A | HIS452 |
A | THR456 |
A | HOH2365 |
A | HOH2410 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1532 |
Chain | Residue |
A | ARG466 |
A | HOH2412 |
B | LYS518 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1528 |
Chain | Residue |
B | ASP13 |
B | ASP14 |
B | DDZ51 |
B | ASP317 |
B | ASN318 |
B | SO41529 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 B 1529 |
Chain | Residue |
B | ASP13 |
B | ASP14 |
B | THR50 |
B | DDZ51 |
B | MET72 |
B | LYS113 |
B | HIS115 |
B | GLY138 |
B | HIS211 |
B | LYS375 |
B | CA1528 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 1530 |
Chain | Residue |
B | THR262 |
B | ARG263 |
B | HOH2201 |
B | HOH2394 |
B | HOH2395 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 1531 |
Chain | Residue |
B | ARG438 |
B | HIS452 |
B | THR456 |
B | HOH2396 |
B | HOH2397 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1532 |
Chain | Residue |
A | ARG428 |
B | ARG428 |
B | HOH2328 |
B | HOH2398 |
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 | CSA1 |
Number of Residues | 7 |
Details | a catalytic site defined by CSA, PubMed 11435113, 10212197 |
Chain | Residue | Details |
A | DDZ51 | |
A | LYS375 | |
A | HIS211 | |
A | LYS113 | |
A | ASP317 | |
A | ARG55 | |
A | HIS115 |
site_id | CSA2 |
Number of Residues | 6 |
Details | a catalytic site defined by CSA, PubMed 11435113, 10212197 |
Chain | Residue | Details |
B | LYS375 | |
B | LYS113 | |
B | HIS211 | |
B | ASP317 | |
B | HIS115 | |
B | ARG55 |
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 |