3MN3
An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGSFGKVKlAyhtttgqk..........VALK |
Chain | Residue | Details |
A | LEU61-LYS84 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLL |
Chain | Residue | Details |
A | ILE173-LEU185 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP177 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU61 | |
A | LYS84 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:11486005, ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:22019086, ECO:0000269|PubMed:26394309, ECO:0000269|PubMed:7905477 |
Chain | Residue | Details |
A | THR210 |