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7MN5

Structure of the HER2/HER3/NRG1b Heterodimer Extracellular Domain

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_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 Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12154198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20696930","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MZW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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