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6LW5

Crystal structure of the human formyl peptide receptor 2 in complex with WKYMVm

Functional Information from GO Data
ChainGOidnamespacecontents
A0001540molecular_functionamyloid-beta binding
A0001774biological_processmicroglial cell activation
A0002376biological_processimmune system process
A0002430biological_processcomplement receptor mediated signaling pathway
A0002768biological_processimmune response-regulating cell surface receptor signaling pathway
A0004875molecular_functioncomplement receptor activity
A0004930molecular_functionG protein-coupled receptor activity
A0004982molecular_functionN-formyl peptide receptor activity
A0005124molecular_functionscavenger receptor binding
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006898biological_processreceptor-mediated endocytosis
A0006935biological_processchemotaxis
A0006954biological_processinflammatory response
A0007154biological_processcell communication
A0007155biological_processcell adhesion
A0007165biological_processsignal transduction
A0007166biological_processcell surface receptor signaling pathway
A0007186biological_processG protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
A0007204biological_processpositive regulation of cytosolic calcium ion concentration
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0019722biological_processcalcium-mediated signaling
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0023052biological_processsignaling
A0032930biological_processpositive regulation of superoxide anion generation
A0035579cellular_componentspecific granule membrane
A0038023molecular_functionsignaling receptor activity
A0038024molecular_functioncargo receptor activity
A0042597cellular_componentperiplasmic space
A0042742biological_processdefense response to bacterium
A0045087biological_processinnate immune response
A0045089biological_processpositive regulation of innate immune response
A0046872molecular_functionmetal ion binding
A0048143biological_processastrocyte activation
A0050728biological_processnegative regulation of inflammatory response
A0050766biological_processpositive regulation of phagocytosis
A0050786molecular_functionRAGE receptor binding
A0050918biological_processpositive chemotaxis
A0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0070821cellular_componenttertiary granule membrane
A0090026biological_processpositive regulation of monocyte chemotaxis
A0097187biological_processdentinogenesis
A0101003cellular_componentficolin-1-rich granule membrane
A1904646biological_processcellular response to amyloid-beta
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CLR A 1201
ChainResidue
AILE203
ASER215
AILE219
ALEU262
AVAL266

site_idAC2
Number of Residues6
Detailsbinding site for residue CLR A 1202
ChainResidue
AVAL147
ATRP150
AVAL24
AASN66
AMET143
AILE146

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. GSVfLIGFIALDRCIcV
ChainResidueDetails
AGLY111-VAL127

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues13
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues43
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues77
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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