2AKH
Normal mode-based flexible fitted coordinates of a non-translocating SecYEG protein-conducting channel into the cryo-EM map of a SecYEG-nascent chain-70S ribosome complex from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009306 | biological_process | protein secretion |
| A | 0015450 | molecular_function | protein-transporting ATPase activity |
| A | 0016020 | cellular_component | membrane |
| B | 0005048 | molecular_function | signal sequence binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006605 | biological_process | protein targeting |
| B | 0006616 | biological_process | SRP-dependent cotranslational protein targeting to membrane, translocation |
| B | 0006886 | biological_process | intracellular protein transport |
| B | 0008320 | molecular_function | protein transmembrane transporter activity |
| B | 0015031 | biological_process | protein transport |
| B | 0016020 | cellular_component | membrane |
| B | 0031522 | cellular_component | cell envelope Sec protein transport complex |
| B | 0043952 | biological_process | protein transport by the Sec complex |
| B | 0065002 | biological_process | intracellular protein transmembrane transport |
| C | 0006605 | biological_process | protein targeting |
| C | 0006886 | biological_process | intracellular protein transport |
| C | 0008320 | molecular_function | protein transmembrane transporter activity |
| C | 0009306 | biological_process | protein secretion |
| C | 0016020 | cellular_component | membrane |
| X | 0009306 | biological_process | protein secretion |
| X | 0015450 | molecular_function | protein-transporting ATPase activity |
| X | 0016020 | cellular_component | membrane |
| Y | 0005048 | molecular_function | signal sequence binding |
| Y | 0005515 | molecular_function | protein binding |
| Y | 0005886 | cellular_component | plasma membrane |
| Y | 0006605 | biological_process | protein targeting |
| Y | 0006616 | biological_process | SRP-dependent cotranslational protein targeting to membrane, translocation |
| Y | 0006886 | biological_process | intracellular protein transport |
| Y | 0008320 | molecular_function | protein transmembrane transporter activity |
| Y | 0015031 | biological_process | protein transport |
| Y | 0016020 | cellular_component | membrane |
| Y | 0031522 | cellular_component | cell envelope Sec protein transport complex |
| Y | 0043952 | biological_process | protein transport by the Sec complex |
| Y | 0065002 | biological_process | intracellular protein transmembrane transport |
| Z | 0006605 | biological_process | protein targeting |
| Z | 0006886 | biological_process | intracellular protein transport |
| Z | 0008320 | molecular_function | protein transmembrane transporter activity |
| Z | 0009306 | biological_process | protein secretion |
| Z | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00755 |
| Number of Residues | 20 |
| Details | SECY_1 Protein secY signature 1. SIFaLGImPYIsASIIIQLL |
| Chain | Residue | Details |
| Y | SER76-LEU95 |
| site_id | PS00756 |
| Number of Residues | 18 |
| Details | SECY_2 Protein secY signature 2. WLgEqITer.GIGNGiSII |
| Chain | Residue | Details |
| Y | TRP173-ILE190 |
| site_id | PS01067 |
| Number of Residues | 29 |
| Details | SECE_SEC61G Protein secE/sec61-gamma signature. FaREaRteVrKviWPtrqEtlhttLIVAA |
| Chain | Residue | Details |
| Z | PHE71-ALA99 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 132 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 360 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01465","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 256 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 38 |
| Details | Intramembrane: {"description":"Helical; Name=Helix 2B","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 30 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 160 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 32 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 30 |
| Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 32 |
| Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 52 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"2050112","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 72 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"2050112","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
