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7MN8

Structure of the HER2/HER3/NRG1b Heterodimer Extracellular Domain bound to Trastuzumab Fab

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
A0016020cellular_componentmembrane
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0006974biological_processDNA damage response
B0008643biological_processcarbohydrate transport
B0015144molecular_functioncarbohydrate transmembrane transporter activity
B0015768biological_processmaltose transport
B0016020cellular_componentmembrane
B0030288cellular_componentouter membrane-bounded periplasmic space
B0034219biological_processcarbohydrate transmembrane transport
B0034289biological_processdetection of maltose stimulus
B0042597cellular_componentperiplasmic space
B0042956biological_processmaltodextrin transmembrane transport
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
B0055085biological_processtransmembrane transport
B0060326biological_processcell chemotaxis
B1901982molecular_functionmaltose binding
B1990060cellular_componentmaltose transport complex
H0005102molecular_functionsignaling receptor binding
H0007399biological_processnervous system development
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DDDMGDLVDaeEY
ChainResidueDetails
BASP1011-TYR1023

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CkCpnEftGDrC
ChainResidueDetails
HCYS210-CYS221

site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGTVYkGiwipdgenvkip......VAIK
ChainResidueDetails
BLEU726-LYS753

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNVLV
ChainResidueDetails
BLEU841-VAL853

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
DTYR201-HIS207
CTYR192-HIS198

site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
BPRO1155-ASN1172

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues629
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BTHR23-THR652

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BSER653-ILE675

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
BASP845

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU726
BLYS753
AGLN788
AASN834

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR182

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000305|PubMed:32381043
ChainResidueDetails
BTYR877

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20696930, ECO:0007744|PDB:2A91, ECO:0007744|PDB:3MZW
ChainResidueDetails
BASN68
AASN616

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN124
BASN629
AASN408
AASN414
AASN437
AASN469
AASN522
AASN566

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0007744|PDB:1N8Z, ECO:0007744|PDB:1S78, ECO:0007744|PDB:2A91, ECO:0007744|PDB:3N85
ChainResidueDetails
BASN187

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: 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
ChainResidueDetails
BASN259

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15093539, ECO:0000269|PubMed:19299620, ECO:0007744|PDB:1S78
ChainResidueDetails
BASN530

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20696930, ECO:0007744|PDB:3MZW
ChainResidueDetails
BASN571

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PDB entries from 2024-07-24

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