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 | 106 |
| Details | Domain: {"description":"Rubredoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10216292","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1637309","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 54 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 50 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 118 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 48 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 38 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 48 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
