Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033192 | molecular_function | calmodulin-dependent protein phosphatase activity |
| A | 0097720 | biological_process | calcineurin-mediated signaling |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033192 | molecular_function | calmodulin-dependent protein phosphatase activity |
| B | 0097720 | biological_process | calcineurin-mediated signaling |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue FE A 501 |
| Chain | Residue |
| A | ASP90 |
| A | HIS92 |
| A | ASP118 |
| A | ZN502 |
| A | PO4503 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | FE501 |
| A | PO4503 |
| A | ASP118 |
| A | ASN150 |
| A | HIS199 |
| A | HIS281 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 A 503 |
| Chain | Residue |
| A | ASP90 |
| A | HIS92 |
| A | ASP118 |
| A | ARG122 |
| A | ASN150 |
| A | HIS151 |
| A | ARG254 |
| A | HIS281 |
| A | FE501 |
| A | ZN502 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue FE B 501 |
| Chain | Residue |
| B | ASP90 |
| B | HIS92 |
| B | PO4503 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 502 |
| Chain | Residue |
| B | ASP90 |
| B | ASP118 |
| B | ASN150 |
| B | HIS199 |
| B | HIS281 |
| B | PO4503 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 B 503 |
| Chain | Residue |
| B | ASP90 |
| B | HIS92 |
| B | ASP118 |
| B | ARG122 |
| B | ASN150 |
| B | HIS151 |
| B | ARG254 |
| B | HIS281 |
| B | FE501 |
| B | ZN502 |
Functional Information from PROSITE/UniProt
| site_id | PS00125 |
| Number of Residues | 6 |
| Details | SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE |
| Chain | Residue | Details |
| A | LEU147-GLU152 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS151 | |
| B | HIS151 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:5C1V, ECO:0007744|PDB:5SVE, ECO:0007744|PDB:6NUC, ECO:0007744|PDB:6NUU, ECO:0007744|PDB:6UUQ |
| Chain | Residue | Details |
| A | ASP90 | |
| B | ASN150 | |
| B | HIS199 | |
| B | HIS281 | |
| A | HIS92 | |
| A | ASP118 | |
| A | ASN150 | |
| A | HIS199 | |
| A | HIS281 | |
| B | ASP90 | |
| B | HIS92 | |
| B | ASP118 | |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 | |
| Chain | Residue | Details |
| A | TYR224 | |
| B | TYR224 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 406 |
| Chain | Residue | Details |
| A | ASP90 | metal ligand |
| A | HIS281 | metal ligand |
| A | HIS92 | metal ligand |
| A | ASP118 | metal ligand |
| A | ASP121 | electrostatic stabiliser |
| A | ARG122 | transition state stabiliser |
| A | ASN150 | metal ligand |
| A | HIS151 | proton shuttle (general acid/base) |
| A | HIS199 | metal ligand |
| A | ARG254 | transition state stabiliser |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 406 |
| Chain | Residue | Details |
| B | ASP90 | metal ligand |
| B | HIS281 | metal ligand |
| B | HIS92 | metal ligand |
| B | ASP118 | metal ligand |
| B | ASP121 | electrostatic stabiliser |
| B | ARG122 | transition state stabiliser |
| B | ASN150 | metal ligand |
| B | HIS151 | proton shuttle (general acid/base) |
| B | HIS199 | metal ligand |
| B | ARG254 | transition state stabiliser |
