7MN5
Structure of the HER2/HER3/NRG1b Heterodimer Extracellular Domain
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004713 | molecular_function | protein tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
A | 0016020 | cellular_component | membrane |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004713 | molecular_function | protein tyrosine kinase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
B | 0006974 | biological_process | DNA damage response |
B | 0008643 | biological_process | carbohydrate transport |
B | 0015144 | molecular_function | carbohydrate transmembrane transporter activity |
B | 0015768 | biological_process | maltose transport |
B | 0016020 | cellular_component | membrane |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0034219 | biological_process | carbohydrate transmembrane transport |
B | 0034289 | biological_process | detection of maltose stimulus |
B | 0042597 | cellular_component | periplasmic space |
B | 0042956 | biological_process | maltodextrin transmembrane transport |
B | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
B | 0055052 | cellular_component | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing |
B | 0055085 | biological_process | transmembrane transport |
B | 0060326 | biological_process | cell chemotaxis |
B | 1901982 | molecular_function | maltose binding |
B | 1990060 | cellular_component | maltose transport complex |
H | 0005102 | molecular_function | signaling receptor binding |
H | 0007399 | biological_process | nervous system development |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DDDMGDLVDaeEY |
Chain | Residue | Details |
B | ASP1011-TYR1023 |
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CkCpnEftGDrC |
Chain | Residue | Details |
H | CYS210-CYS221 |
site_id | PS00107 |
Number of Residues | 28 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGTVYkGiwipdgenvkip......VAIK |
Chain | Residue | Details |
B | LEU726-LYS753 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNVLV |
Chain | Residue | Details |
B | LEU841-VAL853 |
site_id | PS01037 |
Number of Residues | 18 |
Details | SBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN |
Chain | Residue | Details |
B | PRO1155-ASN1172 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12154198","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20696930","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MZW","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PDB","id":"1N8Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S78","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N85","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15093539","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19299620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20696930","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N8Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S78","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A91","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N85","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15093539","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19299620","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S78","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20696930","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MZW","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |