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6AKY

The Crystal structure of Human Chemokine Receptor CCR5 in complex with compound 34

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 2001
ChainResidue
ACYS1006
ACYS1009
ACYS1039
ACYS1042

site_idAC2
Number of Residues2
Detailsbinding site for residue OLC A 2002
ChainResidue
APRO250
AILE253

site_idAC3
Number of Residues12
Detailsbinding site for residue A4X A 2003
ChainResidue
APHE109
APHE112
APHE182
ALYS191
ATHR195
AILE198
ATYR251
ATHR259
AGLU283
ATYR37
ATYR89
ATYR108

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues27
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AARG31-TYR58

site_idSWS_FT_FI2
Number of Residues25
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ALYS59-TYR68
AASP125-THR141

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

site_idSWS_FT_FI14
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00241, ECO:0000269|PubMed:10216292
ChainResidueDetails
ACYS1006
ACYS1009
ACYS1039
ACYS1042

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: N-formylmethionine => ECO:0000269|PubMed:1637309
ChainResidueDetails
AMET1001

222415

PDB entries from 2024-07-10

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