3H9R
Crystal structure of the kinase domain of type I activin receptor (ACVR1) in complex with FKBP12 and dorsomorphin
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 | 0003007 | biological_process | heart morphogenesis |
| B | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| B | 0005160 | molecular_function | transforming growth factor beta receptor binding |
| B | 0005246 | molecular_function | calcium channel regulator activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005527 | molecular_function | macrolide binding |
| B | 0005528 | molecular_function | FK506 binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006457 | biological_process | protein folding |
| B | 0006458 | biological_process | 'de novo' protein folding |
| B | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
| B | 0014802 | cellular_component | terminal cisterna |
| B | 0014809 | biological_process | regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion |
| B | 0016020 | cellular_component | membrane |
| B | 0016529 | cellular_component | sarcoplasmic reticulum |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030018 | cellular_component | Z disc |
| B | 0030512 | biological_process | negative regulation of transforming growth factor beta receptor signaling pathway |
| B | 0030547 | molecular_function | signaling receptor inhibitor activity |
| B | 0032880 | biological_process | regulation of protein localization |
| B | 0032926 | biological_process | negative regulation of activin receptor signaling pathway |
| B | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| B | 0034713 | molecular_function | type I transforming growth factor beta receptor binding |
| B | 0042026 | biological_process | protein refolding |
| B | 0042110 | biological_process | T cell activation |
| B | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| B | 0044325 | molecular_function | transmembrane transporter binding |
| B | 0050776 | biological_process | regulation of immune response |
| B | 0051604 | biological_process | protein maturation |
| B | 0055010 | biological_process | ventricular cardiac muscle tissue morphogenesis |
| B | 0060347 | biological_process | heart trabecula formation |
| B | 0070411 | molecular_function | I-SMAD binding |
| B | 0070697 | molecular_function | activin receptor binding |
| B | 0097435 | biological_process | supramolecular fiber organization |
| B | 0098562 | cellular_component | cytoplasmic side of membrane |
| B | 1902991 | biological_process | regulation of amyloid precursor protein catabolic process |
| B | 1990000 | biological_process | amyloid fibril formation |
| B | 1990425 | cellular_component | ryanodine receptor complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE TAK A 1 |
| Chain | Residue |
| A | VAL175 |
| A | HIS286 |
| A | GLU287 |
| A | GLY289 |
| A | LEU343 |
| A | HOH576 |
| A | GLY176 |
| A | GLU212 |
| A | VAL214 |
| A | ALA233 |
| A | LYS235 |
| A | THR283 |
| A | HIS284 |
| A | TYR285 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 500 |
| Chain | Residue |
| A | HOH121 |
| A | HOH122 |
| A | HOH123 |
| A | HIS284 |
| A | HIS286 |
| A | LYS345 |
| A | LYS346 |
| A | HOH518 |
| A | HOH559 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2 |
| Chain | Residue |
| A | HOH43 |
| A | HOH93 |
| A | ARG380 |
| A | ASN437 |
| A | ASP438 |
| A | PRO439 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3 |
| Chain | Residue |
| A | ARG206 |
| A | SER272 |
| B | GLN54 |
| B | HOH138 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 4 |
| Chain | Residue |
| A | SER440 |
| A | ARG490 |
| A | LYS493 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 5 |
| Chain | Residue |
| A | ARG218 |
| A | LYS338 |
| A | HOH512 |
| A | HOH513 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PG4 A 6 |
| Chain | Residue |
| A | HOH11 |
| A | LEU184 |
| A | GLU230 |
| A | ASN231 |
| A | LEU263 |
| A | GLY264 |
| A | HIS284 |
| A | HIS286 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PG4 A 7 |
| Chain | Residue |
| A | HOH45 |
| A | HOH80 |
| A | THR179 |
| A | LEU210 |
| A | TRP223 |
| A | GLU230 |
| A | ILE236 |
| A | GLN278 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 A 8 |
| Chain | Residue |
| A | TYR432 |
| A | ASP433 |
| A | VAL435 |
| A | ASN437 |
| A | LYS497 |
| A | HOH568 |
| A | HOH569 |
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 | 29 |
| Details | Domain: {"description":"GS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00585","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 88 |
| Details | Domain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26883","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1d6o |
| Chain | Residue | Details |
| B | ASP38 | |
| B | TYR83 | |
| B | ILE57 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1d6o |
| Chain | Residue | Details |
| A | LYS340 | |
| A | ASP336 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1d6o |
| Chain | Residue | Details |
| A | LYS338 | |
| A | ASP336 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1d6o |
| Chain | Residue | Details |
| A | LYS338 | |
| A | ASP336 | |
| A | THR378 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1d6o |
| Chain | Residue | Details |
| A | LYS338 | |
| A | ASP336 | |
| A | ASN341 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 362 |
| Chain | Residue | Details |
| B | TYR27 | electrostatic destabiliser, steric role |
| B | PHE37 | electrostatic destabiliser, polar/non-polar interaction, steric role |
| B | ASP38 | electrostatic stabiliser, steric role |
| B | ILE57 | electrostatic stabiliser, steric role |
| B | TYR83 | electrostatic stabiliser, steric role |
| B | PHE100 | electrostatic destabiliser, polar/non-polar interaction, steric role |
