5C1V
CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 284 |
| Details | Region: {"description":"Catalytic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Region: {"description":"Interaction with PxIxIF motif in substrate","evidences":[{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17502104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Motif: {"description":"SAPNY motif","evidences":[{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31375679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UUQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P63328","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
