eF-site ID 1a16-A PDB Code 1a16 Chain A click to enlarge Title AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU Classification HYDROLASE/HYDROLASE INHIBITOR Compound AMINOPEPTIDASE P Source ORGANISM_SCIENTIFIC: Escherichia coli; Sequence A:  SEISRQEFQRRRQALVEQMQPGSAALIFAAPEVTRSADSE YPYRQNSDFWYFTGFNEPEAVLVLIKSDDTHNHSVLFNRV RDLTAEIWFGRRLGQDAAPEKLGVDRALAFSEINQQLYQL LNGLDVVYHAQGEYAYADVIVNSLEKLRKGSRQNLTAPAT MIDWRPVVHEMRLFKSPEEIAVLRRAGEITAMAHTRAMEK CRPGMFEYHLEGEIHHEFNRHGARYPSYNTIVGSGENGCI LHYTENECEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGK FTQAQREIYDIVLESLETSLRLYRPGTSILEVTGEVVRIM VSGLVKLGILKGDVDELIAQNAHRPFFMHGLSHWLGLDVH DVGVYGQDRSRILEPGMVLTVEPGLYIAPDAEVPEQYRGI GIRIEDDIVITETGNENLTASVVKKPEEIEALMVAARKQ Description Functional site 1) chain A residue 260 type sequence D description THESE RESIDUES COORDINATE THE MN IONS. source : NUL 2) chain A residue 271 type sequence D description THESE RESIDUES COORDINATE THE MN IONS. source : NUL 3) chain A residue 354 type sequence H description THESE RESIDUES COORDINATE THE MN IONS. source : NUL 4) chain A residue 383 type sequence E description THESE RESIDUES COORDINATE THE MN IONS. source : NUL 5) chain A residue 406 type sequence E description THESE RESIDUES COORDINATE THE MN IONS. source : NUL 6) chain A residue 271 type sequence D description BINDING SITE FOR RESIDUE MN A 443 source : AC1 7) chain A residue 354 type sequence H description BINDING SITE FOR RESIDUE MN A 443 source : AC1 8) chain A residue 383 type sequence E description BINDING SITE FOR RESIDUE MN A 443 source : AC1 9) chain A residue 406 type sequence E description BINDING SITE FOR RESIDUE MN A 443 source : AC1 10) chain A residue 229 type sequence Y description BINDING SITE FOR RESIDUE MN A 444 source : AC2 11) chain A residue 260 type sequence D description BINDING SITE FOR RESIDUE MN A 444 source : AC2 12) chain A residue 271 type sequence D description BINDING SITE FOR RESIDUE MN A 444 source : AC2 13) chain A residue 273 type sequence T description BINDING SITE FOR RESIDUE MN A 444 source : AC2 14) chain A residue 406 type sequence E description BINDING SITE FOR RESIDUE MN A 444 source : AC2 15) chain A residue 88 type sequence W description BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 source : AC3 16) chain A residue 153 type sequence R description BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 source : AC3 17) chain A residue 243 type sequence H description BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 source : AC3 18) chain A residue 350 type sequence H description BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 source : AC3 19) chain A residue 351 type sequence G description BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 source : AC3 20) chain A residue 354 type sequence H description BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 source : AC3 21) chain A residue 361 type sequence H description BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 source : AC3 22) chain A residue 370 type sequence R description BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 source : AC3 23) chain A residue 383 type sequence E description BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 source : AC3 24) chain A residue 404 type sequence R description BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 source : AC3 25) chain A residue 39 type catalytic sequence S description 379 source MCSA : MCSA1 26) chain A residue 405 type catalytic sequence I description 379 source MCSA : MCSA1 27) chain A residue 407 type catalytic sequence D description 379 source MCSA : MCSA1 28) chain A residue 244 type catalytic sequence Y description 379 source MCSA : MCSA1 29) chain A residue 261 type catalytic sequence A description 379 source MCSA : MCSA1 30) chain A residue 272 type catalytic sequence I description 379 source MCSA : MCSA1 31) chain A residue 351 type catalytic sequence G description 379 source MCSA : MCSA1 32) chain A residue 355 type catalytic sequence W description 379 source MCSA : MCSA1 33) chain A residue 362 type catalytic sequence D description 379 source MCSA : MCSA1 34) chain A residue 384 type catalytic sequence P description 379 source MCSA : MCSA1 35) chain A residue 388 type catalytic sequence I description 379 source MCSA : MCSA1 36) chain A residue 350-362 type prosite sequence HGLSHWLGLDVHD description PROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGLSHwLGLdVHD source prosite : PS00491 37) chain A residue 261 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI1 38) chain A residue 272 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI1 39) chain A residue 355 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI1 40) chain A residue 384 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI1 41) chain A residue 407 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1

Display surface Download Links