5OXG
Crystal structure of the ACVR1 (ALK2) kinase in complex with LDN-212854
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004675 | molecular_function | transmembrane receptor protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007178 | biological_process | cell surface receptor protein serine/threonine kinase signaling pathway |
| A | 0016020 | cellular_component | membrane |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004675 | molecular_function | transmembrane receptor protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007178 | biological_process | cell surface receptor protein serine/threonine kinase signaling pathway |
| B | 0016020 | cellular_component | membrane |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004675 | molecular_function | transmembrane receptor protein serine/threonine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0007178 | biological_process | cell surface receptor protein serine/threonine kinase signaling pathway |
| C | 0016020 | cellular_component | membrane |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004675 | molecular_function | transmembrane receptor protein serine/threonine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0007178 | biological_process | cell surface receptor protein serine/threonine kinase signaling pathway |
| D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue B4B A 501 |
| Chain | Residue |
| A | VAL214 |
| A | GLY289 |
| A | ASP293 |
| A | ASN341 |
| A | LEU343 |
| A | HOH626 |
| A | HOH630 |
| A | HOH650 |
| A | HOH682 |
| A | VAL222 |
| A | ALA233 |
| A | LEU263 |
| A | THR283 |
| A | HIS284 |
| A | TYR285 |
| A | HIS286 |
| A | GLU287 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | THR203 |
| A | ASP269 |
| A | MET270 |
| A | THR271 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 503 |
| Chain | Residue |
| A | GLU413 |
| A | ARG416 |
| A | TYR427 |
| A | LYS428 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue B4B B 501 |
| Chain | Residue |
| A | PHE462 |
| B | VAL214 |
| B | VAL222 |
| B | ALA233 |
| B | LEU263 |
| B | THR283 |
| B | HIS284 |
| B | TYR285 |
| B | HIS286 |
| B | GLU287 |
| B | GLY289 |
| B | ASP293 |
| B | ASN341 |
| B | LEU343 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CA B 502 |
| Chain | Residue |
| B | GLU413 |
| B | ARG416 |
| B | TYR427 |
| B | LYS428 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | binding site for residue B4B C 501 |
| Chain | Residue |
| C | VAL214 |
| C | VAL222 |
| C | ALA233 |
| C | LYS235 |
| C | LEU263 |
| C | THR283 |
| C | HIS284 |
| C | TYR285 |
| C | HIS286 |
| C | GLU287 |
| C | GLY289 |
| C | ASP293 |
| C | LYS340 |
| C | ASN341 |
| C | LEU343 |
| C | HOH631 |
| C | HOH656 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CA C 503 |
| Chain | Residue |
| C | GLU413 |
| C | ARG416 |
| C | TYR427 |
| C | LYS428 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for residue B4B D 501 |
| Chain | Residue |
| D | VAL214 |
| D | VAL222 |
| D | ALA233 |
| D | LEU263 |
| D | THR283 |
| D | HIS284 |
| D | TYR285 |
| D | HIS286 |
| D | GLU287 |
| D | GLY289 |
| D | ASP293 |
| D | ASN341 |
| D | LEU343 |
| D | HOH612 |
| D | HOH656 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| D | LYS493 |
| D | THR496 |
| D | LYS497 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CA D 503 |
| Chain | Residue |
| D | GLU413 |
| D | ARG416 |
| D | TYR427 |
| D | LYS428 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 22 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGKGRYGEVWrGswqgen............VAVK |
| Chain | Residue | Details |
| A | VAL214-LYS235 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKskNILV |
| Chain | Residue | Details |
| A | ILE332-VAL344 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP336 | |
| B | ASP336 | |
| C | ASP336 | |
| D | ASP336 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | VAL214 | |
| A | LYS235 | |
| B | VAL214 | |
| B | LYS235 | |
| C | VAL214 | |
| C | LYS235 | |
| D | VAL214 | |
| D | LYS235 |
