eF-site ID 5f34-ABCD PDB Code 5f34 Chain A, B, C, D click to enlarge Title Crystal structure of membrane associated PatA from Mycobacterium smegmatis in complex with S-hexadecyl Coenzyme A - P21 space group Classification TRANSFERASE Compound Phosphatidylinositol mannoside acyltransferase Source Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) (ACYLT_MYCS2) Sequence A:  PEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFR LPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGN WDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGF EVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQ VDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMR VYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQ WIADLSDERRARL B:  PEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFR LPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGN WDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGF EVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQ VDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMR VYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQ WIADLSDERRARL C:  PEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFR LPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGN WDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGF EVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQ VDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMR VYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQ WIADLSDERRAR D:  PEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFR LPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGN WDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGF EVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQ VDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMR VYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQ WIADLSDERRARL Description Functional site 1) chain A residue 122 type sequence L description binding site for residue HD6 A 401 source : AC1 2) chain A residue 124 type sequence L description binding site for residue HD6 A 401 source : AC1 3) chain A residue 130 type sequence W description binding site for residue HD6 A 401 source : AC1 4) chain A residue 146 type sequence T description binding site for residue HD6 A 401 source : AC1 5) chain A residue 147 type sequence V description binding site for residue HD6 A 401 source : AC1 6) chain A residue 164 type sequence R description binding site for residue HD6 A 401 source : AC1 7) chain A residue 182 type sequence F description binding site for residue HD6 A 401 source : AC1 8) chain A residue 196 type sequence C description binding site for residue HD6 A 401 source : AC1 9) chain A residue 198 type sequence M description binding site for residue HD6 A 401 source : AC1 10) chain A residue 206 type sequence S description binding site for residue HD6 A 401 source : AC1 11) chain A residue 220 type sequence P description binding site for residue HD6 A 401 source : AC1 12) chain A residue 222 type sequence G description binding site for residue HD6 A 401 source : AC1 13) chain A residue 229 type sequence E description binding site for residue HD6 A 401 source : AC1 14) chain B residue 130 type sequence W description binding site for residue HD6 B 401 source : AC2 15) chain B residue 133 type sequence A description binding site for residue HD6 B 401 source : AC2 16) chain B residue 134 type sequence G description binding site for residue HD6 B 401 source : AC2 17) chain B residue 146 type sequence T description binding site for residue HD6 B 401 source : AC2 18) chain B residue 147 type sequence V description binding site for residue HD6 B 401 source : AC2 19) chain B residue 149 type sequence E description binding site for residue HD6 B 401 source : AC2 20) chain B residue 164 type sequence R description binding site for residue HD6 B 401 source : AC2 21) chain B residue 196 type sequence C description binding site for residue HD6 B 401 source : AC2 22) chain B residue 198 type sequence M description binding site for residue HD6 B 401 source : AC2 23) chain B residue 220 type sequence P description binding site for residue HD6 B 401 source : AC2 24) chain B residue 222 type sequence G description binding site for residue HD6 B 401 source : AC2 25) chain C residue 124 type sequence L description binding site for residue HD6 C 401 source : AC3 26) chain C residue 130 type sequence W description binding site for residue HD6 C 401 source : AC3 27) chain C residue 133 type sequence A description binding site for residue HD6 C 401 source : AC3 28) chain C residue 134 type sequence G description binding site for residue HD6 C 401 source : AC3 29) chain C residue 196 type sequence C description binding site for residue HD6 C 401 source : AC3 30) chain C residue 198 type sequence M description binding site for residue HD6 C 401 source : AC3 31) chain C residue 202 type sequence D description binding site for residue HD6 C 401 source : AC3 32) chain C residue 220 type sequence P description binding site for residue HD6 C 401 source : AC3 33) chain C residue 222 type sequence G description binding site for residue HD6 C 401 source : AC3 34) chain D residue 130 type sequence W description binding site for residue HD6 D 401 source : AC4 35) chain D residue 146 type sequence T description binding site for residue HD6 D 401 source : AC4 36) chain D residue 147 type sequence V description binding site for residue HD6 D 401 source : AC4 37) chain D residue 149 type sequence E description binding site for residue HD6 D 401 source : AC4 38) chain D residue 164 type sequence R description binding site for residue HD6 D 401 source : AC4 39) chain D residue 182 type sequence F description binding site for residue HD6 D 401 source : AC4 40) chain D residue 196 type sequence C description binding site for residue HD6 D 401 source : AC4 41) chain D residue 198 type sequence M description binding site for residue HD6 D 401 source : AC4 42) chain D residue 201 type sequence R description binding site for residue HD6 D 401 source : AC4 43) chain D residue 202 type sequence D description binding site for residue HD6 D 401 source : AC4 44) chain D residue 220 type sequence P description binding site for residue HD6 D 401 source : AC4 45) chain D residue 222 type sequence G description binding site for residue HD6 D 401 source : AC4 46) chain A residue 126 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 126 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694 source Swiss-Prot : SWS_FT_FI1 48) chain C residue 126 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694 source Swiss-Prot : SWS_FT_FI1 49) chain D residue 126 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 200 type ACT_SITE sequence E description ACT_SITE => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 200 type ACT_SITE sequence E description ACT_SITE => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694 source Swiss-Prot : SWS_FT_FI2 52) chain C residue 200 type ACT_SITE sequence E description ACT_SITE => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694 source Swiss-Prot : SWS_FT_FI2 53) chain D residue 200 type ACT_SITE sequence E description ACT_SITE => ECO:0000305|PubMed:26965057, ECO:0000305|PubMed:29185694 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 126 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 55) chain C residue 164 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 56) chain C residue 206 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 57) chain C residue 229 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 58) chain D residue 126 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 59) chain D residue 164 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 60) chain D residue 206 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 61) chain D residue 229 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 62) chain A residue 164 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 63) chain A residue 206 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 64) chain A residue 229 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 65) chain B residue 126 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 66) chain B residue 164 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 67) chain B residue 206 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 68) chain B residue 229 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 69) chain C residue 126 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3

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