eF-site ID 5dir-C PDB Code 5dir Chain C click to enlarge Title membrane protein at 2.8 Angstroms Classification HYDROLASE Compound Lipoprotein signal peptidase Source (5DIR) Sequence C:  PWLWITVLVFVLDQVSKAFFQAELSMYQQIVVIPDLFSWT LAYNTGAAFSFLADSSGWQRWLFALIAIVVSASLVVWLKR LKKGETWLAIALALVLGGALGNLYDRMVLGHVVDFILVHW QNRWYFPAFNLADSAITVGAVMLALDMFR Description Functional site 1) chain C residue 32 type sequence A description binding site for residue OLC B 204 source : AD1 2) chain C residue 14 type sequence W description binding site for residue OLC B 205 source : AD2 3) chain C residue 28 type sequence A description binding site for residue OLC B 205 source : AD2 4) chain C residue 114 type sequence Y description binding site for residue OLC B 205 source : AD2 5) chain C residue 41 type sequence V description binding site for residue OLC C 201 source : AD5 6) chain C residue 42 type sequence V description binding site for residue OLC C 201 source : AD5 7) chain C residue 20 type sequence F description binding site for residue OLC C 202 source : AD6 8) chain C residue 110 type sequence L description binding site for residue OLC C 202 source : AD6 9) chain C residue 114 type sequence Y description binding site for residue OLC C 202 source : AD6 10) chain C residue 117 type sequence M description binding site for residue OLC C 202 source : AD6 11) chain C residue 118 type sequence V description binding site for residue OLC C 202 source : AD6 12) chain C residue 70 type sequence R description binding site for residue OLC C 203 source : AD7 13) chain C residue 78 type sequence I description binding site for residue OLC C 203 source : AD7 14) chain C residue 85 type sequence V description binding site for residue OLC C 203 source : AD7 15) chain C residue 117 type sequence M description binding site for residue OLC C 203 source : AD7 16) chain C residue 29 type sequence F description binding site for residue OLC C 204 source : AD8 17) chain C residue 40 type sequence I description binding site for residue OLC C 204 source : AD8 18) chain C residue 49 type sequence W description binding site for residue OLC C 204 source : AD8 19) chain C residue 65 type sequence S description binding site for residue OLC D 204 source : AE3 20) chain C residue 71 type sequence W description binding site for residue OLC D 204 source : AE3 21) chain C residue 117 type sequence M description binding site for residue OLC D 204 source : AE3 22) chain C residue 19 type sequence V description binding site for residue OLC F 301 source : AE5 23) chain C residue 137 type sequence P description binding site for residue OLC F 301 source : AE5 24) chain C residue 139 type sequence F description binding site for residue OLC F 301 source : AE5 25) chain C residue 143 type sequence D description binding site for residue OLC F 301 source : AE5 26) chain C residue 147 type sequence T description binding site for residue OLC F 301 source : AE5 27) chain C residue 148 type sequence V description binding site for residue OLC F 301 source : AE5 28) chain C residue 153 type sequence L description binding site for residue OLC F 302 source : AE6 29) chain C residue 54 type sequence N description binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 source : AE8 30) chain C residue 56 type sequence G description binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 source : AE8 31) chain C residue 59 type sequence F description binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 source : AE8 32) chain C residue 73 type sequence F description binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 source : AE8 33) chain C residue 112 type sequence N description binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 source : AE8 34) chain C residue 116 type sequence R description binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 source : AE8 35) chain C residue 122 type sequence V description binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 source : AE8 36) chain C residue 124 type sequence D description binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 source : AE8 37) chain C residue 140 type sequence N description binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 source : AE8 38) chain C residue 143 type sequence D description binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 source : AE8 39) chain C residue 90-96 type TOPO_DOM sequence RLKKGET description Cytoplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI1 40) chain C residue 31-67 type TOPO_DOM sequence QAELSMYQQIVVIPDLFSWTLAYNTGAAFSFLADSSG description Periplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI3 41) chain C residue 119-140 type TOPO_DOM sequence LGHVVDFILVHWQNRWYFPAFN description Periplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI3 42) chain C residue 68-89 type TRANSMEM sequence WQRWLFALIAIVVSASLVVWLK description Helical => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI4 43) chain C residue 97-118 type TRANSMEM sequence WLAIALALVLGGALGNLYDRMV description Helical => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS source Swiss-Prot : SWS_FT_FI4 44) chain C residue 141-154 type TRANSMEM sequence LADSAITVGAVMLA description Helical => ECO:0000269|PubMed:26912896, ECO:0007744|PDB:5DIR source Swiss-Prot : SWS_FT_FI5 45) chain C residue 124 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:26912896 source Swiss-Prot : SWS_FT_FI7 46) chain C residue 143 type ACT_SITE sequence D description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:26912896 source Swiss-Prot : SWS_FT_FI7

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