3Q4U
Crystal structure of the ACVR1 kinase domain in complex with LDN-193189
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 | 16 |
| Details | BINDING SITE FOR RESIDUE LDN A 3 |
| Chain | Residue |
| A | VAL214 |
| A | GLY289 |
| A | ASP293 |
| A | LYS340 |
| A | ASN341 |
| A | LEU343 |
| A | HOH555 |
| A | HOH836 |
| A | VAL222 |
| A | ALA233 |
| A | LEU263 |
| A | THR283 |
| A | HIS284 |
| A | TYR285 |
| A | HIS286 |
| A | GLU287 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1 |
| Chain | Residue |
| A | ASP207 |
| A | THR209 |
| A | SER226 |
| A | TRP227 |
| A | GLN228 |
| A | HOH564 |
| C | VAL419 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 2 |
| Chain | Residue |
| A | THR271 |
| A | SER276 |
| A | GLN278 |
| A | HOH1113 |
| C | LDN4 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 500 |
| Chain | Residue |
| A | EDO4 |
| A | TYR294 |
| A | THR299 |
| A | LEU300 |
| A | ASP301 |
| A | SER304 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 4 |
| Chain | Residue |
| A | THR299 |
| A | EDO500 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 5 |
| Chain | Residue |
| A | ARG380 |
| A | ASP438 |
| A | HOH929 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FLC A 501 |
| Chain | Residue |
| A | HOH163 |
| A | HIS284 |
| A | TYR285 |
| A | HIS286 |
| A | GLU287 |
| A | LYS345 |
| A | LYS346 |
| A | FLC502 |
| A | HOH1127 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FLC A 502 |
| Chain | Residue |
| A | HOH119 |
| A | HIS259 |
| A | GLU260 |
| A | ILE262 |
| A | LEU263 |
| A | GLY264 |
| A | HIS284 |
| A | HIS286 |
| A | LYS345 |
| A | FLC501 |
| A | HOH1128 |
| A | HOH1129 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE LDN B 1 |
| Chain | Residue |
| B | VAL214 |
| B | VAL222 |
| B | ALA233 |
| B | LEU263 |
| B | THR283 |
| B | HIS284 |
| B | TYR285 |
| B | HIS286 |
| B | GLU287 |
| B | GLY289 |
| B | LYS340 |
| B | ASN341 |
| B | LEU343 |
| B | HOH564 |
| B | HOH833 |
| B | HOH972 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 7 |
| Chain | Residue |
| B | ILE262 |
| B | LEU263 |
| B | GLY264 |
| B | HIS284 |
| B | HIS286 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 8 |
| Chain | Residue |
| B | TYR294 |
| B | THR299 |
| B | LEU300 |
| B | ASP301 |
| B | SER304 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FLC B 5 |
| Chain | Residue |
| B | HIS284 |
| B | TYR285 |
| B | HIS286 |
| B | GLU287 |
| B | LYS345 |
| B | LYS346 |
| B | HOH971 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FLC B 6 |
| Chain | Residue |
| B | HIS318 |
| B | LEU489 |
| B | LYS492 |
| B | HOH552 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FLC B 500 |
| Chain | Residue |
| B | THR487 |
| B | ALA488 |
| B | LEU489 |
| B | HOH514 |
| B | HOH565 |
| B | HOH979 |
| B | HOH1133 |
| D | ASN481 |
| D | SER483 |
| B | ILE321 |
| B | LYS400 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FLC B 501 |
| Chain | Residue |
| B | LYS338 |
| B | LYS340 |
| B | THR378 |
| B | ARG380 |
| B | ASN437 |
| B | ASP438 |
| B | PRO439 |
| B | HOH555 |
| B | HOH984 |
| site_id | BC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE LDN C 4 |
| Chain | Residue |
| A | EDO2 |
| A | ARG273 |
| A | SER276 |
| C | HOH59 |
| C | VAL222 |
| C | ALA233 |
| C | LEU263 |
| C | THR283 |
| C | HIS284 |
| C | TYR285 |
| C | HIS286 |
| C | GLU287 |
| C | GLY289 |
| C | ASP293 |
| C | LYS340 |
| C | ASN341 |
| C | LEU343 |
| C | HOH537 |
| C | HOH846 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 9 |
| Chain | Residue |
| C | LYS243 |
| C | PHE246 |
| C | ARG247 |
| C | GLU250 |
| C | HOH521 |
| D | HOH35 |
| D | ASN372 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 10 |
| Chain | Residue |
| C | MET360 |
| C | SER362 |
| C | GLN367 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 11 |
| Chain | Residue |
| C | ASP269 |
| C | THR271 |
| C | GLN278 |
| C | TRP280 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FLC C 3 |
| Chain | Residue |
| C | FLC12 |
| C | HOH93 |
| C | HOH165 |
| C | HIS284 |
| C | TYR285 |
| C | HIS286 |
| C | GLU287 |
| C | LYS345 |
| C | LYS346 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FLC C 500 |
| Chain | Residue |
| C | HOH143 |
| C | LYS338 |
| C | LYS340 |
| C | ARG380 |
| C | ASP438 |
| C | PRO439 |
| C | HOH624 |
| C | HOH1108 |
| site_id | CC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FLC C 12 |
| Chain | Residue |
| C | FLC3 |
| C | HOH155 |
| C | ARG258 |
| C | HIS259 |
| C | GLU260 |
| C | ILE262 |
| C | GLY264 |
| C | HIS284 |
| C | HIS286 |
| C | LYS345 |
| C | CYS351 |
| C | HOH1083 |
| site_id | CC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE LDN D 2 |
| 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 | LYS340 |
| D | ASN341 |
| D | LEU343 |
| D | HOH556 |
| D | HOH847 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 6 |
| Chain | Residue |
| D | THR299 |
| D | LEU300 |
| D | ASP301 |
| D | VAL419 |
| site_id | CC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 12 |
| Chain | Residue |
| D | PHE431 |
| D | ASP433 |
| D | GLN453 |
| D | ARG454 |
| D | ASN456 |
| D | HOH551 |
| D | HOH562 |
| D | HOH1111 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 13 |
| Chain | Residue |
| D | HOH30 |
| D | ARG380 |
| D | ASN437 |
| D | ASP438 |
| D | PRO439 |
| D | HOH1064 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 14 |
| Chain | Residue |
| D | TRP227 |
| D | GLN228 |
| D | GLU230 |
| site_id | DC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FLC D 9 |
| Chain | Residue |
| D | HIS284 |
| D | TYR285 |
| D | HIS286 |
| D | GLU287 |
| D | LYS345 |
| D | LYS346 |
| D | HOH501 |
| D | HOH521 |
| D | HOH574 |
| D | HOH619 |
| site_id | DC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FLC D 10 |
| Chain | Residue |
| D | HIS259 |
| D | GLU260 |
| D | ILE262 |
| D | GLY264 |
| D | HIS284 |
| D | HIS286 |
| D | LYS345 |
| D | HOH619 |
| site_id | DC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FLC D 11 |
| Chain | Residue |
| B | SER483 |
| B | ALA484 |
| D | HOH52 |
| D | LYS400 |
| D | THR487 |
| D | ALA488 |
| D | LEU489 |
| D | HOH1067 |
| D | HOH1152 |
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 |
