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8U4R

Structure of REGN7663-Fab bound CXCR4

Functional Information from GO Data
ChainGOidnamespacecontents
R0001618molecular_functionvirus receptor activity
R0001666biological_processresponse to hypoxia
R0001764biological_processneuron migration
R0002064biological_processepithelial cell development
R0002407biological_processdendritic cell chemotaxis
R0003674molecular_functionmolecular_function
R0003779molecular_functionactin binding
R0004930molecular_functionG protein-coupled receptor activity
R0005515molecular_functionprotein binding
R0005575cellular_componentcellular_component
R0005737cellular_componentcytoplasm
R0005764cellular_componentlysosome
R0005768cellular_componentendosome
R0005769cellular_componentearly endosome
R0005770cellular_componentlate endosome
R0005886cellular_componentplasma membrane
R0006091biological_processgeneration of precursor metabolites and energy
R0006915biological_processapoptotic process
R0006954biological_processinflammatory response
R0006955biological_processimmune response
R0007186biological_processG protein-coupled receptor signaling pathway
R0007204biological_processpositive regulation of cytosolic calcium ion concentration
R0007420biological_processbrain development
R0008038biological_processneuron recognition
R0008218biological_processbioluminescence
R0009615biological_processresponse to virus
R0009897cellular_componentexternal side of plasma membrane
R0009986cellular_componentcell surface
R0014070biological_processresponse to organic cyclic compound
R0014823biological_processresponse to activity
R0015026molecular_functioncoreceptor activity
R0016020cellular_componentmembrane
R0016477biological_processcell migration
R0016493molecular_functionC-C chemokine receptor activity
R0016494molecular_functionC-X-C chemokine receptor activity
R0019722biological_processcalcium-mediated signaling
R0019955molecular_functioncytokine binding
R0019957molecular_functionC-C chemokine binding
R0022008biological_processneurogenesis
R0022029biological_processtelencephalon cell migration
R0030155biological_processregulation of cell adhesion
R0030335biological_processpositive regulation of cell migration
R0031252cellular_componentcell leading edge
R0031410cellular_componentcytoplasmic vesicle
R0031625molecular_functionubiquitin protein ligase binding
R0032027molecular_functionmyosin light chain binding
R0032991cellular_componentprotein-containing complex
R0035470biological_processpositive regulation of vascular wound healing
R0036094molecular_functionsmall molecule binding
R0038147molecular_functionC-X-C motif chemokine 12 receptor activity
R0038160biological_processCXCL12-activated CXCR4 signaling pathway
R0043067biological_processregulation of programmed cell death
R0043130molecular_functionubiquitin binding
R0043217biological_processmyelin maintenance
R0045446biological_processendothelial cell differentiation
R0046718biological_processsymbiont entry into host cell
R0048714biological_processpositive regulation of oligodendrocyte differentiation
R0050769biological_processpositive regulation of neurogenesis
R0050792biological_processregulation of viral process
R0050920biological_processregulation of chemotaxis
R0050921biological_processpositive regulation of chemotaxis
R0050965biological_processdetection of temperature stimulus involved in sensory perception of pain
R0050966biological_processdetection of mechanical stimulus involved in sensory perception of pain
R0051924biological_processregulation of calcium ion transport
R0060048biological_processcardiac muscle contraction
R0060326biological_processcell chemotaxis
R0061154biological_processendothelial tube morphogenesis
R0070062cellular_componentextracellular exosome
R0070098biological_processchemokine-mediated signaling pathway
R0070161cellular_componentanchoring junction
R0071345biological_processcellular response to cytokine stimulus
R0071417biological_processcellular response to organonitrogen compound
R0071466biological_processcellular response to xenobiotic stimulus
R0120162biological_processpositive regulation of cold-induced thermogenesis
R1901327biological_processresponse to tacrolimus
R1903861biological_processpositive regulation of dendrite extension
R1904018biological_processpositive regulation of vasculature development
R1905322biological_processpositive regulation of mesenchymal stem cell migration
R1990478biological_processresponse to ultrasound
R2000448biological_processpositive regulation of macrophage migration inhibitory factor signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SSVlILAFISLDRYLaI
ChainResidueDetails
RSER122-ILE138

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCNVDH
ChainResidueDetails
HTYR207-HIS213
LTYR197-HIS203

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:20929726
ChainResidueDetails
RILE39-MET63

site_idSWS_FT_FI2
Number of Residues109
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:20929726
ChainResidueDetails
RGLY64-ARG77
RSER131-LYS154
RSER217-THR241
RALA303-SER352

site_idSWS_FT_FI3
Number of Residues21
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:20929726
ChainResidueDetails
RLEU78-VAL99

site_idSWS_FT_FI4
Number of Residues50
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:20929726
ChainResidueDetails
RALA100-LYS110
RALA175-TRP195
RASP262-LYS282

site_idSWS_FT_FI5
Number of Residues19
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:20929726
ChainResidueDetails
RALA111-ILE130

site_idSWS_FT_FI6
Number of Residues19
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:20929726
ChainResidueDetails
RVAL155-PHE174

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:20929726
ChainResidueDetails
RVAL196-LEU216

site_idSWS_FT_FI8
Number of Residues19
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:20929726
ChainResidueDetails
RVAL242-ILE261

site_idSWS_FT_FI9
Number of Residues19
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:20929726
ChainResidueDetails
RTRP283-TYR302

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Chemokine binding
ChainResidueDetails
RASP171

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Chemokine binding => ECO:0000269|PubMed:20929726, ECO:0000305|PubMed:10825158
ChainResidueDetails
RGLU288

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Sulfotyrosine; partial => ECO:0000269|PubMed:18834145
ChainResidueDetails
RTYR7
RTYR12

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Sulfotyrosine => ECO:0000269|PubMed:12034737, ECO:0000269|PubMed:16725153, ECO:0000269|PubMed:18834145
ChainResidueDetails
RTYR21

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
RSER319
RSER348

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20048153, ECO:0007744|PubMed:23186163
ChainResidueDetails
RSER321

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC and GRK6 => ECO:0000269|PubMed:19116316, ECO:0000269|PubMed:20048153, ECO:0007744|PubMed:23186163
ChainResidueDetails
RSER324
RSER325

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphoserine; by GRK6 => ECO:0000269|PubMed:20048153
ChainResidueDetails
RSER330
RSER339

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20048153
ChainResidueDetails
RSER351

site_idSWS_FT_FI19
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10756055
ChainResidueDetails
RASN11

site_idSWS_FT_FI20
Number of Residues1
DetailsCARBOHYD: O-linked (Xyl...) (chondroitin sulfate) serine => ECO:0000269|PubMed:12034737
ChainResidueDetails
RSER18

site_idSWS_FT_FI21
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN176

site_idSWS_FT_FI22
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:28978524
ChainResidueDetails
RLYS331

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132
ChainResidueDetails
RTYR434

site_idSWS_FT_FI24
Number of Residues2
DetailsCROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132
ChainResidueDetails
RTHR433
RGLY435

222926

PDB entries from 2024-07-24

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