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 | 629 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
B | THR23-THR652 |
site_id | SWS_FT_FI2 |
Number of Residues | 22 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
B | SER653-ILE675 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
Chain | Residue | Details |
B | ASP845 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
B | LEU726 | |
B | LYS753 | |
A | GLN788 | |
A | ASN834 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | THR182 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000305|PubMed:32381043 |
Chain | Residue | Details |
B | TYR877 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20696930, ECO:0007744|PDB:2A91, ECO:0007744|PDB:3MZW |
Chain | Residue | Details |
B | ASN68 | |
A | ASN616 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN124 | |
B | ASN629 | |
A | ASN408 | |
A | ASN414 | |
A | ASN437 | |
A | ASN469 | |
A | ASN522 | |
A | ASN566 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0007744|PDB:1N8Z, ECO:0007744|PDB:1S78, ECO:0007744|PDB:2A91, ECO:0007744|PDB:3N85 |
Chain | Residue | Details |
B | ASN187 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15093539, ECO:0000269|PubMed:19299620, ECO:0000269|PubMed:20696930, ECO:0007744|PDB:1N8Z, ECO:0007744|PDB:1S78, ECO:0007744|PDB:2A91, ECO:0007744|PDB:3MZW, ECO:0007744|PDB:3N85 |
Chain | Residue | Details |
B | ASN259 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15093539, ECO:0000269|PubMed:19299620, ECO:0007744|PDB:1S78 |
Chain | Residue | Details |
B | ASN530 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20696930, ECO:0007744|PDB:3MZW |
Chain | Residue | Details |
B | ASN571 |