6AKX
The Crystal structure of Human Chemokine Receptor CCR5 in complex with compound 21
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0004950 | molecular_function | chemokine receptor activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0006935 | biological_process | chemotaxis |
A | 0006954 | biological_process | inflammatory response |
A | 0006955 | biological_process | immune response |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016020 | cellular_component | membrane |
A | 0016493 | molecular_function | C-C chemokine receptor activity |
A | 0043448 | biological_process | alkane catabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004930 | molecular_function | G protein-coupled receptor activity |
B | 0004950 | molecular_function | chemokine receptor activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0006935 | biological_process | chemotaxis |
B | 0006954 | biological_process | inflammatory response |
B | 0006955 | biological_process | immune response |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0009055 | molecular_function | electron transfer activity |
B | 0016020 | cellular_component | membrane |
B | 0016493 | molecular_function | C-C chemokine receptor activity |
B | 0043448 | biological_process | alkane catabolic process |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 2001 |
Chain | Residue |
A | CYS1006 |
A | CYS1009 |
A | CYS1039 |
A | CYS1042 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue NO3 A 2002 |
Chain | Residue |
A | ASP76 |
A | GLY111 |
A | HIS289 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue A4R A 2003 |
Chain | Residue |
A | TYR108 |
A | PHE109 |
A | PHE112 |
A | THR195 |
A | TYR251 |
A | LEU255 |
A | GLU283 |
A | TYR37 |
A | TRP86 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN B 2001 |
Chain | Residue |
B | CYS1006 |
B | CYS1009 |
B | CYS1039 |
B | CYS1042 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue NO3 B 2002 |
Chain | Residue |
B | ASP76 |
B | TRP248 |
B | HIS289 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for residue A4R B 2003 |
Chain | Residue |
B | TYR37 |
B | TRP86 |
B | TYR89 |
B | PHE109 |
B | PHE112 |
B | THR195 |
B | ILE198 |
B | TYR251 |
B | LEU255 |
B | GLU283 |
B | MET287 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 54 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
A | ARG31-TYR58 | |
B | ARG31-TYR58 |
site_id | SWS_FT_FI2 |
Number of Residues | 50 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | LYS59-TYR68 | |
A | ASP125-THR141 | |
B | LYS59-TYR68 | |
B | ASP125-THR141 |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
A | LEU69-TYR89 | |
B | LEU69-TYR89 |
site_id | SWS_FT_FI4 |
Number of Residues | 118 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | ALA90-GLN102 | |
A | THR167-ILE198 | |
A | GLN261-GLN277 | |
B | ALA90-GLN102 | |
B | THR167-ILE198 | |
B | GLN261-GLN277 |
site_id | SWS_FT_FI5 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
A | LEU103-ILE124 | |
B | LEU103-ILE124 |
site_id | SWS_FT_FI6 |
Number of Residues | 48 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
A | VAL142-PHE166 | |
B | VAL142-PHE166 |
site_id | SWS_FT_FI7 |
Number of Residues | 38 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
A | VAL199-LEU218 | |
B | VAL199-LEU218 |
site_id | SWS_FT_FI8 |
Number of Residues | 48 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
A | LEU236-PHE260 | |
B | LEU236-PHE260 |
site_id | SWS_FT_FI9 |
Number of Residues | 46 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
A | ALA278-GLY301 | |
B | ALA278-GLY301 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Sulfotyrosine => ECO:0000269|PubMed:10089882 |
Chain | Residue | Details |
A | TYR3 | |
B | TYR3 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: Sulfotyrosine => ECO:0000269|PubMed:21763489 |
Chain | Residue | Details |
A | TYR10 | |
A | TYR14 | |
B | TYR10 | |
B | TYR14 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Sulfotyrosine => ECO:0000255 |
Chain | Residue | Details |
A | TYR15 | |
B | TYR15 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | CARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:11733580 |
Chain | Residue | Details |
A | SER6 | |
A | SER7 | |
B | SER6 | |
B | SER7 |
site_id | SWS_FT_FI14 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00241, ECO:0000269|PubMed:10216292 |
Chain | Residue | Details |
A | CYS1006 | |
A | CYS1009 | |
A | CYS1039 | |
A | CYS1042 | |
B | CYS1006 | |
B | CYS1009 | |
B | CYS1039 | |
B | CYS1042 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: N-formylmethionine => ECO:0000269|PubMed:1637309 |
Chain | Residue | Details |
A | MET1001 | |
B | MET1001 |