1ARM
CARBOXYPEPTIDASE A WITH ZN REPLACED BY HG
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG A 310 |
| Chain | Residue |
| A | HIS69 |
| A | GLU72 |
| A | HIS196 |
| A | TRS319 |
| A | HOH320 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU A 315 |
| Chain | Residue |
| A | GLU270 |
| A | TRS319 |
| A | HOH320 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HG A 316 |
| Chain | Residue |
| A | GLU28 |
| A | HIS29 |
| A | LYS84 |
| A | THR87 |
| A | GLU88 |
| A | THR4 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE HG A 317 |
| Chain | Residue |
| A | HOH376 |
| A | HOH446 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE HG A 318 |
| Chain | Residue |
| A | HIS29 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TRS A 319 |
| Chain | Residue |
| A | HIS69 |
| A | ARG71 |
| A | GLU72 |
| A | ARG127 |
| A | HIS196 |
| A | SER197 |
| A | TYR198 |
| A | GLU270 |
| A | PHE279 |
| A | HG310 |
| A | CU315 |
| A | HOH320 |
| A | HOH321 |
Functional Information from PROSITE/UniProt
| site_id | PS00132 |
| Number of Residues | 23 |
| Details | CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF |
| Chain | Residue | Details |
| A | PRO60-PHE82 |
| site_id | PS00133 |
| Number of Residues | 11 |
| Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY |
| Chain | Residue | Details |
| A | HIS196-TYR206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 293 |
| Details | Domain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12431056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IY7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12431056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IY7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| A | ARG127 | |
| A | GLU270 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbx |
| Chain | Residue | Details |
| A | ARG71 | |
| A | GLU270 | |
| A | ARG127 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 171 |
| Chain | Residue | Details |
| A | HIS69 | metal ligand |
| A | GLU72 | metal ligand |
| A | ARG127 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS196 | metal ligand |
| A | GLU270 | covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor |
