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5WB2

US28 bound to engineered chemokine CX3CL1.35 and nanobodies

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004950molecular_functionchemokine receptor activity
A0006935biological_processchemotaxis
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
B0005576cellular_componentextracellular region
B0006955biological_processimmune response
B0008009molecular_functionchemokine activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue CLR A 1201
ChainResidue
AILE239
APRO243
ALEU246
APHE265
AALA272
ACLR1202
ACLR1202

site_idAC2
Number of Residues6
Detailsbinding site for residue CLR A 1202
ChainResidue
AALA272
ALEU275
ACLR1201
ACLR1201
ASER268
AARG271

site_idAC3
Number of Residues7
Detailsbinding site for residue OLC A 1203
ChainResidue
APHE46
AARG225
AARG228
AARG228
AVAL229
AALA232
ALEU286

site_idAC4
Number of Residues6
Detailsbinding site for residue OLC A 1204
ChainResidue
AVAL102
ALEU106
AARG139
APHE150
APHE154
AOLC1206

site_idAC5
Number of Residues6
Detailsbinding site for residue OLC A 1205
ChainResidue
AILE73
ALEU80
ALEU81
ALEU106
ACYS110
APHE150

site_idAC6
Number of Residues5
Detailsbinding site for residue OLC A 1206
ChainResidue
APHE116
ATHR123
ATRP151
AGLY195
AOLC1204

site_idAC7
Number of Residues3
Detailsbinding site for residue ZN B 101
ChainResidue
BVAL21
BHIS64
DGLU44

site_idAC8
Number of Residues9
Detailsbinding site for residue MES B 102
ChainResidue
ATHR108
ACYS173
ATHR175
ATYR177
BLEU1
BLEU2
BPRO3
BHIS4
BASN6

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASLcFITEIALDRYYaI
ChainResidueDetails
AALA117-ILE133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues49
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues45
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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