6ALZ
Crystal structure of Protein Phosphatase 1 bound to the natural inhibitor Tautomycetin
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MN A 401 |
Chain | Residue |
A | ASP92 |
A | ASN124 |
A | HIS173 |
A | HIS248 |
A | MN402 |
A | HOH543 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MN A 402 |
Chain | Residue |
A | MN401 |
A | HOH504 |
A | HOH543 |
A | ASP64 |
A | HIS66 |
A | ASP92 |
site_id | AC3 |
Number of Residues | 17 |
Details | binding site for residue BKM A 403 |
Chain | Residue |
A | ARG96 |
A | CYS127 |
A | SER129 |
A | TYR134 |
A | VAL195 |
A | TRP206 |
A | ARG221 |
A | VAL223 |
A | HIS248 |
A | VAL250 |
A | TYR272 |
A | PHE276 |
A | HOH504 |
A | HOH530 |
A | HOH543 |
A | HOH547 |
A | HOH570 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue DMS A 404 |
Chain | Residue |
A | PRO50 |
A | GLU54 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CL A 405 |
Chain | Residue |
A | GLY215 |
A | GLY228 |
A | GLU230 |
A | VAL231 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue CL A 406 |
Chain | Residue |
A | LYS297 |
A | HOH664 |
B | PHE257 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue CL A 407 |
Chain | Residue |
A | GLN294 |
A | ILE295 |
B | HOH512 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue MN B 401 |
Chain | Residue |
B | ASP64 |
B | HIS66 |
B | ASP92 |
B | MN402 |
B | HOH510 |
B | HOH546 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MN B 402 |
Chain | Residue |
B | ASP92 |
B | ASN124 |
B | HIS173 |
B | HIS248 |
B | MN401 |
B | HOH510 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue CL B 404 |
Chain | Residue |
B | GLY215 |
B | GLY228 |
B | ALA229 |
B | GLU230 |
B | VAL231 |
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 | LEU121-GLU126 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P36873","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"30100357","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35830882","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35831509","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36175670","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39446389","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8SW5","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |