Structure of PDB 3fcx Chain A

Receptor sequence
>3fcxA (length=268) Species: 9606 (Homo sapiens) [Search protein sequence]
MALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYW
LSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIFGTGAGFYVD
ATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALIC
ALKNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGSKWKAYDATHLVKSY
PLDILIDQGKDDQFLLDGQLLPDNFIAACTEKKIPVVFRLQEDYDHSYYF
IATFITDHIRHHAKYLNA
3D structure
PDB3fcx Crystal structure of human esterase D: a potential genetic marker of retinoblastoma
ChainA
Resolution1.5 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.1.1.56: methylumbelliferyl-acetate deacetylase.
3.1.2.12: S-formylglutathione hydrolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG A H153 P178 D203 A204 H145 P170 D192 A193
BS02 CA A D226 Q227 D259 H260 D212 Q213 D245 H246
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016788 hydrolase activity, acting on ester bonds
GO:0018738 S-formylglutathione hydrolase activity
GO:0042802 identical protein binding
GO:0047374 methylumbelliferyl-acetate deacetylase activity
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0008150 biological_process
GO:0046294 formaldehyde catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005788 endoplasmic reticulum lumen
GO:0005829 cytosol
GO:0031410 cytoplasmic vesicle
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3fcx, PDBe:3fcx, PDBj:3fcx
PDBsum3fcx
PubMed19126594
UniProtP10768|ESTD_HUMAN S-formylglutathione hydrolase (Gene Name=ESD)

[Back to BioLiP]