1IAS
CYTOPLASMIC DOMAIN OF UNPHOSPHORYLATED TYPE I TGF-BETA RECEPTOR CRYSTALLIZED WITHOUT FKBP12
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 |
E | 0004672 | molecular_function | protein kinase activity |
E | 0004675 | molecular_function | transmembrane receptor protein serine/threonine kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006468 | biological_process | protein phosphorylation |
E | 0007178 | biological_process | cell surface receptor protein serine/threonine kinase signaling pathway |
E | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 1 |
Chain | Residue |
E | HIS283 |
E | LYS342 |
E | LYS343 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 E 2 |
Chain | Residue |
E | LYS337 |
E | ARG377 |
E | SER434 |
E | ASP435 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 4 |
Chain | Residue |
C | LYS223 |
C | GLN208 |
C | ARG221 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 5 |
Chain | Residue |
C | LYS337 |
C | ARG377 |
C | ASP435 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 6 |
Chain | Residue |
B | TYR282 |
B | HIS283 |
B | LYS342 |
B | LYS343 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 9 |
Chain | Residue |
A | TYR282 |
A | HIS283 |
A | LYS342 |
A | LYS343 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 10 |
Chain | Residue |
C | TYR282 |
C | HIS283 |
C | LYS342 |
C | LYS343 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 11 |
Chain | Residue |
B | ARG221 |
B | LYS223 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 12 |
Chain | Residue |
B | LYS337 |
B | ARG377 |
B | LEU426 |
B | ASP435 |
B | PRO436 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 13 |
Chain | Residue |
D | TYR282 |
D | HIS283 |
D | LYS342 |
D | LYS343 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 14 |
Chain | Residue |
D | LYS337 |
D | ARG377 |
D | LEU426 |
D | ASP435 |
D | PRO436 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 D 15 |
Chain | Residue |
D | ARG221 |
D | LYS223 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 18 |
Chain | Residue |
A | ARG221 |
A | LYS223 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 E 20 |
Chain | Residue |
E | ARG221 |
E | LYS223 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 21 |
Chain | Residue |
A | LYS337 |
A | ARG377 |
A | LEU426 |
A | SER434 |
A | ASP435 |
A | PRO436 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 22 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGRFGEVWrGkwrgee............VAVK |
Chain | Residue | Details |
A | ILE211-LYS232 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKskNILV |
Chain | Residue | Details |
A | ILE329-VAL341 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP333 | |
B | ASP333 | |
C | ASP333 | |
D | ASP333 | |
E | ASP333 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | ILE211 | |
E | LYS232 | |
A | LYS232 | |
B | ILE211 | |
B | LYS232 | |
C | ILE211 | |
C | LYS232 | |
D | ILE211 | |
D | LYS232 | |
E | ILE211 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | SER165 | |
B | SER165 | |
C | SER165 | |
D | SER165 | |
E | SER165 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | MOD_RES: Phosphothreonine; by TGFBR2 => ECO:0000269|PubMed:7774578 |
Chain | Residue | Details |
A | THR185 | |
E | THR186 | |
A | THR186 | |
B | THR185 | |
B | THR186 | |
C | THR185 | |
C | THR186 | |
D | THR185 | |
D | THR186 | |
E | THR185 |
site_id | SWS_FT_FI5 |
Number of Residues | 15 |
Details | MOD_RES: Phosphoserine; by TGFBR2 => ECO:0000269|PubMed:7774578 |
Chain | Residue | Details |
A | SER187 | |
D | SER187 | |
D | SER189 | |
D | SER191 | |
E | SER187 | |
E | SER189 | |
E | SER191 | |
A | SER189 | |
A | SER191 | |
B | SER187 | |
B | SER189 | |
B | SER191 | |
C | SER187 | |
C | SER189 | |
C | SER191 |
site_id | SWS_FT_FI6 |
Number of Residues | 10 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250 |
Chain | Residue | Details |
A | LYS391 | |
B | LYS391 | |
C | LYS391 | |
D | LYS391 | |
E | LYS391 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS337 | |
A | ASP333 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
E | LYS335 | |
E | ASP333 |
site_id | CSA11 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR375 | |
A | LYS335 | |
A | ASP333 |
site_id | CSA12 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | THR375 | |
B | LYS335 | |
B | ASP333 |
site_id | CSA13 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | THR375 | |
C | LYS335 | |
C | ASP333 |
site_id | CSA14 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
D | THR375 | |
D | LYS335 | |
D | ASP333 |
site_id | CSA15 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
E | THR375 | |
E | LYS335 | |
E | ASP333 |
site_id | CSA16 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASN338 | |
A | LYS335 | |
A | ASP333 |
site_id | CSA17 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASN338 | |
B | LYS335 | |
B | ASP333 |
site_id | CSA18 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | ASN338 | |
C | LYS335 | |
C | ASP333 |
site_id | CSA19 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
D | ASN338 | |
D | LYS335 | |
D | ASP333 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | LYS337 | |
B | ASP333 |
site_id | CSA20 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
E | ASN338 | |
E | LYS335 | |
E | ASP333 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | LYS337 | |
C | ASP333 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
D | LYS337 | |
D | ASP333 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
E | LYS337 | |
E | ASP333 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS335 | |
A | ASP333 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | LYS335 | |
B | ASP333 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | LYS335 | |
C | ASP333 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
D | LYS335 | |
D | ASP333 |