7JUK
Crystal structure of PTEN with a tetra-phosphorylated tail (4p-crPTEN-13sp-T2, SDTTDSDPENEG)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004725 | molecular_function | protein tyrosine phosphatase activity |
A | 0006470 | biological_process | protein dephosphorylation |
A | 0008285 | biological_process | negative regulation of cell population proliferation |
A | 0016311 | biological_process | dephosphorylation |
A | 0016314 | molecular_function | phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity |
A | 0016791 | molecular_function | phosphatase activity |
A | 0046856 | biological_process | phosphatidylinositol dephosphorylation |
A | 0051717 | molecular_function | inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity |
A | 0051800 | molecular_function | phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue PO4 A 401 |
Chain | Residue |
A | GLU43 |
A | LYS332 |
A | HOH501 |
Functional Information from PROSITE/UniProt
site_id | PS00383 |
Number of Residues | 11 |
Details | TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. IHCkaGkgRTG |
Chain | Residue | Details |
A | ILE122-GLY132 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00590 |
Chain | Residue | Details |
A | CYS124 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08586 |
Chain | Residue | Details |
A | LEU318 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:26166433 |
Chain | Residue | Details |
A | THR321 | |
A | THR319 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by FRK => ECO:0000269|PubMed:19345329 |
Chain | Residue | Details |
A | TYR336 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by ROCK1 and CK2 => ECO:0000269|PubMed:11035045 |
Chain | Residue | Details |
A | SER367 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by ROCK1 and CK2 => ECO:0000269|PubMed:11035045 |
Chain | Residue | Details |
A | THR370 | |
A | THR369 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:11035045, ECO:0000269|PubMed:12297295 |
Chain | Residue | Details |
A | SER372 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18716620 |
Chain | Residue | Details |
A | LYS13 | |
A | LYS313 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 456 |
Chain | Residue | Details |
A | ASP92 | proton shuttle (general acid/base) |
A | CYS124 | covalent catalysis |
A | ARG130 | transition state stabiliser |