6I1S
Crystal structure of the ACVR1 (ALK2) kinase in complex with FKBP12 and the inhibitor E6201
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 | 18 |
| Details | binding site for residue E26 A 501 |
| Chain | Residue |
| A | VAL214 |
| A | GLY289 |
| A | LYS340 |
| A | ASN341 |
| A | LEU343 |
| A | ALA353 |
| A | HOH656 |
| A | HOH667 |
| A | HOH674 |
| A | HOH680 |
| A | TYR219 |
| A | ALA233 |
| A | LYS235 |
| A | THR283 |
| A | HIS284 |
| A | TYR285 |
| A | HIS286 |
| A | GLU287 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | PHE431 |
| A | ASP433 |
| A | GLN453 |
| A | ARG454 |
| A | ASN456 |
| A | HOH666 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | ARG380 |
| A | TYR432 |
| A | VAL435 |
| A | PRO436 |
| A | ASN437 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | ARG380 |
| A | ASP438 |
| A | PRO439 |
| A | HOH625 |
| A | HOH724 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | MET288 |
| A | TYR294 |
| A | LEU297 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | TYR294 |
| A | THR299 |
| A | LEU300 |
| A | SER304 |
| A | HOH641 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | ASN366 |
| A | CYS395 |
| A | PHE396 |
| A | ASP397 |
| A | HOH639 |
| B | ILE8 |
| B | PRO10 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | GLY217 |
| A | ARG218 |
| A | HOH642 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | ASP397 |
| A | SER398 |
| A | ARG401 |
| A | PRO482 |
| A | SER483 |
| B | ILE8 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 510 |
| Chain | Residue |
| A | HIS284 |
| A | HIS286 |
| A | LYS345 |
| A | LYS346 |
| A | HOH601 |
| A | HOH626 |
| A | HOH632 |
| A | HOH704 |
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 | 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_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| 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_FI4 |
| 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 | 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 |
