4MBS
Crystal Structure of the CCR5 Chemokine Receptor
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 | 11 |
| Details | BINDING SITE FOR RESIDUE MRV A 1101 |
| Chain | Residue |
| A | TYR37 |
| A | THR259 |
| A | GLU283 |
| A | TRP86 |
| A | TYR89 |
| A | TYR108 |
| A | PHE109 |
| A | PHE182 |
| A | THR195 |
| A | TRP248 |
| A | TYR251 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1102 |
| Chain | Residue |
| A | CYS1006 |
| A | CYS1009 |
| A | CYS1039 |
| A | CYS1042 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLC A 1103 |
| Chain | Residue |
| A | PHE158 |
| B | PRO35 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 1104 |
| Chain | Residue |
| A | PRO84 |
| A | PHE85 |
| A | HIS88 |
| A | OLC1105 |
| A | HOH1219 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 1105 |
| Chain | Residue |
| A | SER38 |
| A | PRO84 |
| A | HIS88 |
| A | OLC1104 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 1106 |
| Chain | Residue |
| A | PHE78 |
| A | THR99 |
| A | GLN102 |
| A | TRP153 |
| A | HOH1212 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 1107 |
| Chain | Residue |
| A | LEU33 |
| A | VAL281 |
| A | THR284 |
| A | LEU285 |
| A | THR288 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OLC A 1108 |
| Chain | Residue |
| A | TYR214 |
| A | ARG235 |
| A | PHE238 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MRV B 1101 |
| Chain | Residue |
| B | TYR37 |
| B | TRP86 |
| B | TYR89 |
| B | TYR108 |
| B | PHE109 |
| B | PHE182 |
| B | LYS191 |
| B | THR195 |
| B | TRP248 |
| B | TYR251 |
| B | THR259 |
| B | GLU283 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1102 |
| Chain | Residue |
| B | CYS1006 |
| B | CYS1009 |
| B | CYS1039 |
| B | CYS1042 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE OLC B 1103 |
| Chain | Residue |
| B | OLC1105 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC B 1104 |
| Chain | Residue |
| B | ALA30 |
| B | PRO34 |
| B | SER38 |
| B | HOH1210 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLC B 1105 |
| Chain | Residue |
| B | ALA278 |
| B | OLC1103 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC B 1106 |
| Chain | Residue |
| B | VAL234 |
| B | ARG235 |
| B | PHE238 |
| B | HOH1226 |
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 | 150 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| A | LYS59-TYR68 | |
| A | ASP125-THR141 | |
| A | GLU302-LEU352 | |
| B | LYS59-TYR68 | |
| B | ASP125-THR141 | |
| B | GLU302-LEU352 |
| 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 | 8 |
| Details | MOD_RES: Phosphoserine; by BARK1 => ECO:0000269|PubMed:10085131 |
| Chain | Residue | Details |
| A | SER336 | |
| A | SER337 | |
| A | SER342 | |
| A | SER349 | |
| B | SER336 | |
| B | SER337 | |
| B | SER342 | |
| B | SER349 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 6 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:11323418 |
| Chain | Residue | Details |
| A | CYS321 | |
| A | CYS323 | |
| A | CYS324 | |
| B | CYS321 | |
| B | CYS323 | |
| B | CYS324 |
| site_id | SWS_FT_FI15 |
| 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_FI16 |
| 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_FI17 |
| Number of Residues | 2 |
| Details | MOD_RES: N-formylmethionine => ECO:0000269|PubMed:1637309 |
| Chain | Residue | Details |
| A | MET1001 | |
| B | MET1001 |
