eF-site ID 6ie1-A PDB Code 6ie1 Chain A click to enlarge Title Crystal Structure of ELMO2(Engulfment and cell motility protein 2) Classification CELL ADHESION Compound Engulfment and cell motility protein 2 Source (ELMO2_HUMAN) Sequence A:  DIVKVAIEWPGANAQLLEIDQKRPLASIIKEVCDGWSLPN PEYYTLRYADGPQLYITEQTRSDIKNGTILQLAISPSRAA RQLMERTQSSNMETRLDAMKELAKLSADVTFATEFINMDG IIVLTRLVESGTKLLSHYSEMLAFTLTAFLELMDHGIVSW DMVSITFIKQIAGYVSQPMVDVSILQRSLAILESMVLNSQ SLYQKIAEEITVGQLISHLQVSNQEIQTYAIALINALFLK APEDKRQDMANAFAQKHLRSIILNHVIRGNRPIKTEMAHQ LYVLQVLTFNLLEERMMTKMDPNDQAQRDIIFELRRIAFD AESDPSNAPGSGTEKRKAMYTKDYKMLGFTNHINPAMDFT QTPPGMLALDNMLYLAKVHQDTYIRIVLENSSREDKHECP FGRSAIELTKMLCEILQVGELPNEGRNDYHPMFFTHDRAF EELFGICIQLLNKTWKEMRATAEDFNKVMQVVREQITRAL PSKPNSLDQFKSKLRSLSYSEILRLRQS Description Functional site 1) chain A residue 225 type sequence Q description binding site for residue GOL A 601 source : AC1 2) chain A residue 265 type sequence S description binding site for residue GOL A 601 source : AC1 3) chain A residue 266 type sequence I description binding site for residue GOL A 601 source : AC1 4) chain A residue 269 type sequence N description binding site for residue GOL A 601 source : AC1 5) chain A residue 270 type sequence H description binding site for residue GOL A 601 source : AC1 6) chain A residue 289 type sequence L description binding site for residue GOL A 602 source : AC2 7) chain A residue 290 type sequence Q description binding site for residue GOL A 602 source : AC2 8) chain A residue 293 type sequence T description binding site for residue GOL A 602 source : AC2 9) chain A residue 438 type sequence F description binding site for residue GOL A 602 source : AC2 10) chain A residue 439 type sequence F description binding site for residue GOL A 602 source : AC2 11) chain A residue 48 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q8BHL5 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 503 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2

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