4L35
Crystal structure of cruxrhodopsin-3 at pH5 from Haloarcula vallismortis at 2.1 angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005216 | molecular_function | monoatomic ion channel activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0007602 | biological_process | phototransduction |
| A | 0009881 | molecular_function | photoreceptor activity |
| A | 0016020 | cellular_component | membrane |
| A | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE RET A 301 |
| Chain | Residue |
| A | TYR81 |
| A | TRP186 |
| A | TYR189 |
| A | PRO190 |
| A | TRP193 |
| A | LYS220 |
| A | TRP84 |
| A | THR87 |
| A | THR88 |
| A | LEU91 |
| A | MET116 |
| A | TRP142 |
| A | SER145 |
| A | THR146 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 22B A 302 |
| Chain | Residue |
| A | GLY29 |
| A | TRP30 |
| A | TYR41 |
| A | PHE52 |
| A | ASN104 |
| A | THR105 |
| A | LEU112 |
| A | PHE148 |
| A | SER159 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 47 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"25268964","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical; Name=Helix A","evidences":[{"source":"PubMed","id":"25268964","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"25268964","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=Helix B","evidences":[{"source":"PubMed","id":"25268964","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Transmembrane: {"description":"Helical; Name=Helix C","evidences":[{"source":"PubMed","id":"25268964","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=Helix D","evidences":[{"source":"PubMed","id":"25268964","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=Helix E","evidences":[{"source":"PubMed","id":"25268964","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=Helix F","evidences":[{"source":"PubMed","id":"25268964","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=Helix G","evidences":[{"source":"PubMed","id":"25268964","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Site: {"description":"Primary proton acceptor","evidences":[{"source":"UniProtKB","id":"P02945","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(retinylidene)lysine","evidences":[{"source":"PubMed","id":"25268964","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JR8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L35","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
