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3OE0

Crystal structure of the CXCR4 chemokine receptor in complex with a cyclic peptide antagonist CVX15

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0019955molecular_functioncytokine binding
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR CHAIN I OF POLYPHEMUSIN ANALOG, CXC CHEMOKINE RECEPTOR ANTAGONIST
ChainResidue
AHIS113
AASP193
AVAL196
APHE199
AGLN200
AASP262
ALEU266
AGLU277
AHIS281
AILE284
ASER285
ATYR116
AGLU288
IHOH1601
IHOH1602
IHOH1604
ATHR117
AASP171
AASP187
AARG188
APHE189
ATYR190
APRO191

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SSVwILAFISLDRYLaI
ChainResidueDetails
ASER122-ILE138

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues50
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues23
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues3
DetailsRegion: {"description":"Chemokine binding","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10825158","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsRegion: {"description":"Chemokine binding"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues12
DetailsRegion: {"description":"Involved in dimerization; when bound to chemokine"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues4
DetailsRegion: {"description":"Chemokine binding, important for signaling and HIV-1 coreceptor activity"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues21
DetailsRegion: {"description":"Involved in dimerization"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsMotif: {"description":"Important for signaling"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues1
DetailsSite: {"description":"Chemokine binding"}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues1
DetailsSite: {"description":"Chemokine binding","evidences":[{"source":"PubMed","id":"20929726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10825158","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

243531

PDB entries from 2025-10-22

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