3FEE
The high resolution structure of human glutamate carboxypeptidase III (GCPIII/NAALADase II) in complex with quisqualic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 0016805 | molecular_function | dipeptidase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile; for NAALADase activity => ECO:0000250|UniProtKB:Q04609 |
| Chain | Residue | Details |
| A | GLU414 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Charge relay system => ECO:0000255 |
| Chain | Residue | Details |
| A | SER618 | |
| A | ASP656 | |
| A | HIS679 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 13 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3 |
| Chain | Residue | Details |
| A | TYR262 | |
| A | HIS367 | |
| A | ASP377 | |
| A | GLU414 | |
| A | GLU415 | |
| A | GLU423 | |
| A | GLU426 | |
| A | ASP443 | |
| A | HIS543 | |
| A | LYS689 | |
| A | ARG200 | |
| A | ASN247 | |
| A | THR259 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3 |
| Chain | Residue | Details |
| A | SER507 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q04609 |
| Chain | Residue | Details |
| A | TYR542 | |
| A | ARG524 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19678840, ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED, ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3 |
| Chain | Residue | Details |
| A | ASN449 | |
| A | ASN628 | |
| A | ASN111 | |
| A | ASN185 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:Q04609 |
| Chain | Residue | Details |
| A | ASN143 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN603 | |
| A | ASN314 |
