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5UIW

Crystal Structure of CC Chemokine Receptor 5 (CCR5) in complex with high potency HIV entry inhibitor 5P7-CCL5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004950molecular_functionchemokine receptor activity
A0005506molecular_functioniron ion binding
A0006935biological_processchemotaxis
A0006954biological_processinflammatory response
A0006955biological_processimmune response
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0016493molecular_functionC-C chemokine receptor activity
A0043448biological_processalkane catabolic process
A0046872molecular_functionmetal ion binding
B0005576cellular_componentextracellular region
B0006955biological_processimmune response
B0008009molecular_functionchemokine activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1101
ChainResidue
ACYS1006
ACYS1009
ACYS1039
ACYS1042

site_idAC2
Number of Residues6
Detailsbinding site for residue OLC A 1102
ChainResidue
AHOH1230
APHE189
AASN192
APHE193
ALEU196
AOLC1107

site_idAC3
Number of Residues1
Detailsbinding site for residue OLC A 1103
ChainResidue
APHE85

site_idAC4
Number of Residues3
Detailsbinding site for residue OLC A 1104
ChainResidue
AALA249
ALEU266
AARG274

site_idAC5
Number of Residues2
Detailsbinding site for residue OLC A 1105
ChainResidue
AGLN277
AALA278

site_idAC6
Number of Residues2
Detailsbinding site for residue OLC A 1106
ChainResidue
ASER38
AHIS88

site_idAC7
Number of Residues6
Detailsbinding site for residue OLC A 1107
ChainResidue
AASN24
AILE28
ALEU32
APHE189
AGLN277
AOLC1102

site_idAC8
Number of Residues2
Detailsbinding site for residue OLA A 1108
ChainResidue
AARG235
AOLA1109

site_idAC9
Number of Residues2
Detailsbinding site for residue OLA A 1109
ChainResidue
AILE242
AOLA1108

Functional Information from PROSITE/UniProt
site_idPS00202
Number of Residues11
DetailsRUBREDOXIN Rubredoxin signature. IpDDWvCPlCG
ChainResidueDetails
AILE1033-GLY1043

site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SGIfFIILLTIDRYLaV
ChainResidueDetails
ASER114-VAL130

site_idPS00472
Number of Residues42
DetailsSMALL_CYTOKINES_CC Small cytokines (intercrine/chemokine) C-C subfamily signature. CCFayiarp..LprahIkeYfytsgk..Csnp.AVVFvtrknrqv.CA
ChainResidueDetails
BCYS10-ALA51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Methionine sulfoxide => ECO:0000269|PubMed:1380064
ChainResidueDetails
BMET67

site_idSWS_FT_FI2
Number of Residues75
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ALYS59-TYR68
AASP125-THR141
AGLU302-PRO352

site_idSWS_FT_FI3
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
ALEU69-TYR89

site_idSWS_FT_FI4
Number of Residues59
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AALA90-GLN102
ATHR167-ILE198
AGLN261-GLN277

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
ALEU103-ILE124

site_idSWS_FT_FI6
Number of Residues24
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AVAL142-PHE166

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
AVAL199-LEU218

site_idSWS_FT_FI8
Number of Residues24
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
ALEU236-PHE260

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AALA278-GLY301

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Sulfotyrosine => ECO:0000269|PubMed:10089882
ChainResidueDetails
ATYR3

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Sulfotyrosine => ECO:0000269|PubMed:21763489
ChainResidueDetails
ATYR10
ATYR14

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Sulfotyrosine => ECO:0000255
ChainResidueDetails
ATYR15

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphoserine; by BARK1 => ECO:0000269|PubMed:10085131
ChainResidueDetails
ATYR336
ATHR337
AGLU342
ALEU349

site_idSWS_FT_FI14
Number of Residues3
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:11323418
ChainResidueDetails
ACYS321
AILE323
APHE324

site_idSWS_FT_FI15
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:11733580
ChainResidueDetails
ASER6
ASER7

site_idSWS_FT_FI16
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00241, ECO:0000269|PubMed:10216292
ChainResidueDetails
ACYS1006
ACYS1009
ACYS1039
ACYS1042

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: N-formylmethionine => ECO:0000269|PubMed:1637309
ChainResidueDetails
AMET1001

227111

PDB entries from 2024-11-06

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