3FED
The high resolution structure of human glutamate carboxypeptidase III (GCPIII/NAALADase II) in complex with a transition state analog of Glu-Glu
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0004181 | molecular_function | metallocarboxypeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016805 | molecular_function | dipeptidase activity |
| A | 0046395 | biological_process | carboxylic acid catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050129 | molecular_function | N-formylglutamate deformylase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; for NAALADase activity","evidences":[{"source":"UniProtKB","id":"Q04609","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19678840","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FEC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FF3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19678840","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FEC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FF3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q04609","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19678840","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FEC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FF3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"UniProtKB","id":"Q04609","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| A | GLU414 |
