4C02
Crystal structure of human ACVR1 (ALK2) in complex with FKBP12.6 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 | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| B | 0005102 | molecular_function | signaling receptor binding |
| B | 0005246 | molecular_function | calcium channel regulator activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005528 | molecular_function | FK506 binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006457 | biological_process | protein folding |
| B | 0006458 | biological_process | 'de novo' protein folding |
| B | 0010459 | biological_process | negative regulation of heart rate |
| B | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| B | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
| B | 0016020 | cellular_component | membrane |
| B | 0016529 | cellular_component | sarcoplasmic reticulum |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019722 | biological_process | calcium-mediated signaling |
| B | 0019855 | molecular_function | calcium channel inhibitor activity |
| B | 0030018 | cellular_component | Z disc |
| B | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| B | 0034704 | cellular_component | calcium channel complex |
| B | 0042026 | biological_process | protein refolding |
| B | 0044325 | molecular_function | transmembrane transporter binding |
| B | 0050849 | biological_process | negative regulation of calcium-mediated signaling |
| B | 0051280 | biological_process | negative regulation of release of sequestered calcium ion into cytosol |
| B | 0051604 | biological_process | protein maturation |
| B | 0051775 | biological_process | response to redox state |
| B | 0060314 | biological_process | regulation of ryanodine-sensitive calcium-release channel activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FLC A 1500 |
| Chain | Residue |
| A | HIS318 |
| A | ILE321 |
| A | LYS492 |
| A | HOH2036 |
| A | HOH2063 |
| A | HOH2066 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FLC A 1501 |
| Chain | Residue |
| A | HOH2075 |
| B | THR28 |
| B | LYS36 |
| B | SER39 |
| B | ARG41 |
| B | ASP42 |
| A | GLY325 |
| A | GLN363 |
| A | HOH2074 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FLC A 1502 |
| Chain | Residue |
| A | HIS284 |
| A | TYR285 |
| A | HIS286 |
| A | GLU287 |
| A | LYS345 |
| A | LYS346 |
| A | EDO1510 |
| A | HOH2044 |
| A | HOH2045 |
| A | HOH2091 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FLC A 1503 |
| Chain | Residue |
| A | ARG258 |
| A | HIS259 |
| A | GLU260 |
| A | ILE262 |
| A | LEU263 |
| A | GLY264 |
| A | HIS284 |
| A | HIS286 |
| A | LYS345 |
| A | EDO1510 |
| A | EDO1513 |
| A | HOH2183 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FLC A 1504 |
| Chain | Residue |
| A | LYS338 |
| A | LYS340 |
| A | ARG380 |
| A | ASN437 |
| A | ASP438 |
| A | PRO439 |
| A | HOH2109 |
| A | HOH2184 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FLC A 1505 |
| Chain | Residue |
| A | THR487 |
| A | LEU489 |
| A | ARG490 |
| A | LYS493 |
| A | FLC1506 |
| A | HOH2186 |
| B | LYS48 |
| B | GLU108 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FLC A 1506 |
| Chain | Residue |
| A | ILE321 |
| A | LYS400 |
| A | THR487 |
| A | ALA488 |
| A | LEU489 |
| A | FLC1505 |
| A | HOH2125 |
| B | LEU105 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FLC B 1108 |
| Chain | Residue |
| A | MET270 |
| B | ALA82 |
| B | TYR83 |
| B | GLY84 |
| B | ALA85 |
| B | THR86 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TAK A 1507 |
| Chain | Residue |
| A | VAL222 |
| A | ALA233 |
| A | LEU263 |
| A | THR283 |
| A | HIS284 |
| A | TYR285 |
| A | HIS286 |
| A | GLU287 |
| A | GLY289 |
| A | LEU343 |
| A | ASP354 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 1109 |
| Chain | Residue |
| B | LEU31 |
| B | ASN33 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1508 |
| Chain | Residue |
| A | PHE431 |
| A | ASP433 |
| A | ARG454 |
| A | ASN456 |
| A | HOH2138 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 1110 |
| Chain | Residue |
| B | PHE47 |
| B | LYS48 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1509 |
| Chain | Residue |
| A | CYS395 |
| A | ASP397 |
| A | SER398 |
| A | ARG401 |
| A | PRO482 |
| A | SER483 |
| B | ASP12 |
| B | ARG14 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1510 |
| Chain | Residue |
| A | FLC1503 |
| A | GLU260 |
| A | LYS345 |
| A | ASN347 |
| A | FLC1502 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1511 |
| Chain | Residue |
| A | THR302 |
| A | HOH2164 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1512 |
| Chain | Residue |
| A | ARG454 |
| A | PRO455 |
| A | LYS475 |
| A | TRP478 |
| A | HOH2160 |
| A | HOH2170 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1513 |
| Chain | Residue |
| A | PHE265 |
| A | HIS284 |
| A | FLC1503 |
| A | HOH2006 |
| A | HOH2189 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1111 |
| Chain | Residue |
| B | PRO10 |
| B | GLY11 |
| B | SER68 |
| B | GLN71 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1514 |
| Chain | Residue |
| A | ARG206 |
| B | GLN54 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1515 |
| Chain | Residue |
| A | GLU212 |
| A | THR299 |
| A | VAL419 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1516 |
| Chain | Residue |
| A | ASN231 |
| A | GLU287 |
| A | THR298 |
| A | THR299 |
| A | LEU300 |
| A | ASP301 |
| A | SER304 |
| A | HOH2043 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1112 |
| Chain | Residue |
| A | LYS446 |
| A | VAL450 |
| A | ASP451 |
| B | ILE51 |
| B | GLY52 |
| B | GLU61 |
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 |
