eF-site ID 5xey-ABCD PDB Code 5xey Chain A, B, C, D click to enlarge Title Discovery and structural analysis of a phloretin hydrolase from the opportunistic pathogen Mycobacterium abscessus Classification HYDROLASE Compound phloretin hydrolase Source (B1MK49_MYCA9) Sequence A:  VHPITYYPVDTQRLVRSNAERIRHKPYAHYFNPDVAVPEE VFAALKAPLEPEQVLGTSSTELNRLLEPGYLEGETGYCGL PDGAGYTSSLVRFPGATPEMFRWWFWWHSFEPERYSLWHP WCHADIWRTDPETETAPNLTDEQRYVGSTHHINEYIGQDP LDIEITFIDPARWGFDADGFAAAGIGAHACGSVLMKGSHM RLATMVHLARITDDGFELRSRYWIADRAEPRHDPVAGIAQ LTTVPGFSGERQAYEQLVHDQTEFNHLATFLPDIYQE B:  VHPITYYPVDTQRLVRSNAERIRHKPYAHYFNPDVAVPEE VFAALKAPLEPEQVLGTSSTELNRLLEPGYLEGETGYCGL PDGAGYTSSLVRFPGATPEMFRWWFWWHSFEPERYSLWHP WCHADIWRTDPETEDEQRYVGSTHHINEYIGQDPLDIEIT FIDPARWGFDADGFAAAGIGAHACGSVLMKGSHMRLATMV HLARITDDGFELRSRYWIADRAEPRHDPVAGIAQLTTVPG FSGERQAYEQLVHDQTEFNHLATFLPDIYQEFG C:  VHPITYYPVDTQRLVRSNAERIRHKPYAHYFNPDVAVPEE VFAALKAPLEPEQVLGTSSTELNRLLEPGYLEGETGYCGL PDGAGYTSSLVRFPGATPEMFRWWFWWHSFEPERYSLWHP WCHADIWRTSTHHINEYIGQDPLDIEITFIDPARWGFDAD GFAAAGIGAHACGSVLMKGSHMRLATMVHLARITDDGFEL RSRYWIADRAEPRHDPVAGIAQLTTVPGFSGERQAYEQLV HDQTEFNHLATFLPDIYQE D:  HPITYYPVDTQRLVRSNAERIRHKPYAHYFNPDVAVPEEV FAALKAPLEPEQVLGTSSTELNRLLEPGYLEGETGYCGLP DGAGYTSSLVRFPGATPEMFRWWFWWHSFEPERYSLWHPW CHADIWRTPETETAPNTDEQRYVGSTHHINEYIGQDPLDI EITFIDPARWGFDADGFAAAGIGAHACGSVLMKGSHMRLA TMVHLARITDDGFELRSRYWIGERQAYEQLVHDQTEFNHL ATFLPDIYQE Description Functional site 1) chain B residue 115 type sequence F description binding site for residue 83X B 301 source : AC1 2) chain B residue 125 type sequence Y description binding site for residue 83X B 301 source : AC1 3) chain B residue 128 type sequence W description binding site for residue 83X B 301 source : AC1 4) chain B residue 164 type sequence E description binding site for residue 83X B 301 source : AC1 5) chain B residue 175 type sequence I description binding site for residue 83X B 301 source : AC1 6) chain B residue 177 type sequence F description binding site for residue 83X B 301 source : AC1 7) chain B residue 215 type sequence M description binding site for residue 83X B 301 source : AC1 8) chain B residue 217 type sequence H description binding site for residue 83X B 301 source : AC1 9) chain B residue 232 type sequence Y description binding site for residue 83X B 301 source : AC1 10) chain B residue 266 type sequence Q description binding site for residue 83X B 301 source : AC1 11) chain B residue 269 type sequence H description binding site for residue 83X B 301 source : AC1 12) chain A residue 125 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 13) chain D residue 125 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 14) chain D residue 215 type BINDING sequence M description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 15) chain D residue 232 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 215 type BINDING sequence M description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 232 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 125 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 215 type BINDING sequence M description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 232 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 21) chain C residue 125 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 22) chain C residue 215 type BINDING sequence M description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 23) chain C residue 232 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:30784195 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 133 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 25) chain C residue 164 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 26) chain C residue 269 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 273 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 28) chain D residue 133 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 29) chain D residue 164 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 30) chain D residue 269 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 31) chain D residue 273 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 164 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 269 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 273 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 133 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 164 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 269 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 273 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2 39) chain C residue 133 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q4K423 source Swiss-Prot : SWS_FT_FI2

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