3FCX
Crystal structure of human esterase D
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005829 | cellular_component | cytosol |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0018738 | molecular_function | S-formylglutathione hydrolase activity |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046294 | biological_process | formaldehyde catabolic process |
| A | 0047374 | molecular_function | methylumbelliferyl-acetate deacetylase activity |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005788 | cellular_component | endoplasmic reticulum lumen |
| B | 0005829 | cellular_component | cytosol |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0018738 | molecular_function | S-formylglutathione hydrolase activity |
| B | 0031410 | cellular_component | cytoplasmic vesicle |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046294 | biological_process | formaldehyde catabolic process |
| B | 0047374 | molecular_function | methylumbelliferyl-acetate deacetylase activity |
| B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 283 |
| Chain | Residue |
| A | HIS153 |
| A | ILE175 |
| A | PRO178 |
| A | ALA204 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 284 |
| Chain | Residue |
| A | GLN227 |
| A | ASP259 |
| A | HIS260 |
| A | HOH544 |
| A | HOH554 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 283 |
| Chain | Residue |
| B | LYS39 |
| B | PRO46 |
| B | HIS74 |
| B | GLY75 |
| B | ASN281 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 284 |
| Chain | Residue |
| B | GLY104 |
| B | VAL107 |
| B | TYR118 |
| B | MET120 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"19126594","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"Q9R0P3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9R0P3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pfq |
| Chain | Residue | Details |
| A | ASP231 | |
| A | SER149 | |
| A | HIS260 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pfq |
| Chain | Residue | Details |
| B | ASP231 | |
| B | SER149 | |
| B | HIS260 |
