4BD9
Structure of the complex between SmCI and human carboxypeptidase A4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004181 | molecular_function | metallocarboxypeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008270 | molecular_function | zinc ion binding |
| B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0010466 | biological_process | negative regulation of peptidase activity |
| B | 0030414 | molecular_function | peptidase inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | HIS69 |
| A | GLU72 |
| A | HIS196 |
| A | HOH2032 |
| B | ILE1 |
Functional Information from PROSITE/UniProt
| site_id | PS00132 |
| Number of Residues | 23 |
| Details | CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaVwLnaGiHSrEwISQataiwT |
| Chain | Residue | Details |
| A | PRO60-THR82 |
| site_id | PS00133 |
| Number of Residues | 11 |
| Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmYPY |
| Chain | Residue | Details |
| A | HIS196-TYR206 |
| site_id | PS00280 |
| Number of Residues | 19 |
| Details | BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGCqgnanrFetkddC |
| Chain | Residue | Details |
| B | PHE32-CYS50 | |
| B | PHE84-CYS102 | |
| B | PHE143-CYS161 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23746805, ECO:0007744|PDB:4BD9 |
| Chain | Residue | Details |
| B | ILE1 | |
| B | SER2 | |
| B | TYR109 | |
| B | GLN110 | |
| B | LYS111 | |
| B | GLY113 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|Ref.1 |
| Chain | Residue | Details |
| B | ALA23 | |
| A | TYR11 | |
| A | HIS12 | |
| A | SER13 | |
| A | LYS85 | |
| A | ASP158 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17506531, ECO:0007744|PDB:2PCU |
| Chain | Residue | Details |
| A | GLU15 | |
| A | PHE51 | |
| A | ARG84 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:15738388, ECO:0000269|PubMed:16091843, ECO:0000269|PubMed:17506531, ECO:0000269|PubMed:22294694, ECO:0000269|PubMed:23746805, ECO:0007744|PDB:2BO9, ECO:0007744|PDB:2BOA, ECO:0007744|PDB:2PCU, ECO:0007744|PDB:4A94, ECO:0007744|PDB:4BD9 |
| Chain | Residue | Details |
| A | HIS69 | |
| A | GLU72 | |
| A | HIS196 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17506531, ECO:0000269|PubMed:23746805, ECO:0007744|PDB:2PCU, ECO:0007744|PDB:4BD9 |
| Chain | Residue | Details |
| A | SER136 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15738388, ECO:0000269|PubMed:16091843, ECO:0000269|PubMed:17506531, ECO:0007744|PDB:2BO9, ECO:0007744|PDB:2BOA, ECO:0007744|PDB:2PCU |
| Chain | Residue | Details |
| A | ASN148 |
