4BGG
Crystal structure of the ACVR1 kinase in complex with LDN-213844
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 | 13 |
| Details | BINDING SITE FOR RESIDUE 844 A 1000 |
| Chain | Residue |
| A | ALA233 |
| A | LYS340 |
| A | ASN341 |
| A | LEU343 |
| A | HOH2004 |
| A | LYS235 |
| A | GLU248 |
| A | THR283 |
| A | HIS284 |
| A | TYR285 |
| A | HIS286 |
| A | GLY289 |
| A | ASP293 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FLC A 1001 |
| Chain | Residue |
| A | TYR285 |
| A | HIS286 |
| A | GLU287 |
| A | MET288 |
| A | VAL344 |
| A | LYS345 |
| A | LYS346 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FLC A 1002 |
| Chain | Residue |
| A | ARG380 |
| A | ASP438 |
| A | HOH2029 |
| A | HOH2040 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FLC A 1003 |
| Chain | Residue |
| A | ARG247 |
| A | GLU250 |
| A | GLY371 |
| A | ASN372 |
| B | LYS243 |
| B | PHE246 |
| B | ARG247 |
| B | GLU250 |
| B | ASP369 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1004 |
| Chain | Residue |
| A | HIS259 |
| A | GLU260 |
| A | ILE262 |
| A | GLY264 |
| A | HIS286 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 844 B 1000 |
| Chain | Residue |
| B | VAL214 |
| B | ALA233 |
| B | LYS235 |
| B | GLU248 |
| B | LEU281 |
| B | THR283 |
| B | TYR285 |
| B | HIS286 |
| B | LYS340 |
| B | ASN341 |
| B | LEU343 |
| B | ASP354 |
| B | HOH2003 |
| B | HOH2013 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FLC B 1001 |
| Chain | Residue |
| B | TYR285 |
| B | HIS286 |
| B | GLU287 |
| B | LYS345 |
| B | LYS346 |
| B | FLC1002 |
| B | HOH2036 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FLC B 1002 |
| Chain | Residue |
| B | HIS259 |
| B | GLU260 |
| B | ILE262 |
| B | GLY264 |
| B | HIS284 |
| B | HIS286 |
| B | LYS345 |
| B | FLC1001 |
| B | HOH2009 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FLC B 1003 |
| Chain | Residue |
| B | LYS338 |
| B | LYS340 |
| B | THR378 |
| B | ARG380 |
| B | ASN437 |
| B | ASP438 |
| B | PRO439 |
| B | HOH2038 |
| B | HOH2060 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 844 C 1000 |
| Chain | Residue |
| C | ALA233 |
| C | LYS235 |
| C | GLU248 |
| C | LEU281 |
| C | THR283 |
| C | TYR285 |
| C | HIS286 |
| C | ASP293 |
| C | LYS340 |
| C | ASN341 |
| C | LEU343 |
| C | HOH2004 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FLC C 1001 |
| Chain | Residue |
| C | TYR285 |
| C | HIS286 |
| C | GLU287 |
| C | LYS345 |
| C | LYS346 |
| C | HOH2002 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 844 D 1000 |
| Chain | Residue |
| D | LEU281 |
| D | THR283 |
| D | TYR285 |
| D | HIS286 |
| D | GLY289 |
| D | LYS340 |
| D | LEU343 |
| D | HOH2003 |
| D | VAL214 |
| D | ALA233 |
| D | LYS235 |
| D | GLU248 |
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 |
