7LV3
Crystal structure of human protein kinase G (PKG) R-C complex in inhibited state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004692 | molecular_function | cGMP-dependent protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004692 | molecular_function | cGMP-dependent protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGGFGRVElVqlkseeskt.........FAMK |
| Chain | Residue | Details |
| A | LEU381-LYS405 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNLIL |
| Chain | Residue | Details |
| A | ILE495-LEU507 |
| site_id | PS00888 |
| Number of Residues | 17 |
| Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. IIkEGDvGSlVYVMedG |
| Chain | Residue | Details |
| A | ILE145-GLY161 | |
| A | ILE263-GLY279 |
| site_id | PS00889 |
| Number of Residues | 18 |
| Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGElAIlynct......RTAtVkT |
| Chain | Residue | Details |
| A | PHE181-THR198 | |
| A | PHE305-ALA322 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| B | ASP499 | |
| A | ASP499 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21526164, ECO:0007744|PDB:3OD0 |
| Chain | Residue | Details |
| B | GLY182 | |
| B | ARG192 | |
| A | GLY182 | |
| A | ARG192 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24239458, ECO:0000269|PubMed:25271401, ECO:0007744|PDB:4KU7, ECO:0007744|PDB:4QXK |
| Chain | Residue | Details |
| A | ARG316 | |
| A | TYR351 | |
| B | ARG297 | |
| B | GLY306 | |
| B | ARG316 | |
| B | TYR351 | |
| A | ARG297 | |
| A | GLY306 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LEU381 | |
| A | LYS405 | |
| B | LEU381 | |
| B | LYS405 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:P00516 |
| Chain | Residue | Details |
| A | LYS75 | |
| B | LYS75 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0C605 |
| Chain | Residue | Details |
| A | THR530 | |
| B | THR530 |
