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 | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11435113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9748219","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P15289","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11435113","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via 3-oxoalanine","evidences":[{"source":"PubMed","id":"11435113","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"3-oxoalanine (Cys)","evidences":[{"source":"PubMed","id":"11435113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9748219","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 | THR379 | electrostatic stabiliser |
| A | ASP14 | metal ligand |
| A | DDZ51 | covalently attached, increase electrophilicity, metal ligand, nucleophile, proton donor |
| A | LEU59 | electrostatic stabiliser |
| A | GLY117 | electrostatic stabiliser, increase electrophilicity |
| A | LYS119 | electrostatic stabiliser, proton acceptor |
| A | GLN215 | electrostatic stabiliser, proton donor |
| A | GLU321 | activator, increase nucleophilicity, metal ligand, proton acceptor |
| A | GLY322 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 661 |
| Chain | Residue | Details |
| B | ASP13 | metal ligand |
| B | THR379 | electrostatic stabiliser |
| B | ASP14 | metal ligand |
| B | DDZ51 | covalently attached, increase electrophilicity, metal ligand, nucleophile, proton donor |
| B | LEU59 | electrostatic stabiliser |
| B | GLY117 | electrostatic stabiliser, increase electrophilicity |
| B | LYS119 | electrostatic stabiliser, proton acceptor |
| B | GLN215 | electrostatic stabiliser, proton donor |
| B | GLU321 | activator, increase nucleophilicity, metal ligand, proton acceptor |
| B | GLY322 | metal ligand |
