eF-site ID 5f2t-AB PDB Code 5f2t Chain A, B click to enlarge Title Crystal structure of membrane associated PatA from Mycobacterium smegmatis in complex with palmitate - C 2 space group Classification TRANSFERASE Compound Phosphatidylinositol mannoside acyltransferase Source Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) (ACYLT_MYCS2) Sequence A:  GGPEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREA FRLPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHS GNWDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESL GFEVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSG VQVDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWG MRVYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQ PQWIADL B:  ARYAARNGGPEQLRRNLARVVGKPPADVPDDLIRASLASY ARYWREAFRLPAMDHGRLGEQLDVIDIDHLWSALDAGRGA VLALPHSGNWDMAGVWLVQNYGPFTTVAERLKPESLYRRF VEYRESLGFEVLPLTGGERPPFEVLAERLTDNRPICLMAE RDLTRSGVQVDFFGEATRMPAGPAKLAIETGAALFPVHCW FEGDGWGMRVYPELDTSSGDVTAITQALADRFAANIATYP ADWHMLQPQWIADLSDERRARL Description (1)  Phosphatidylinositol mannoside acyltransferase (E.C.2.3.1.-) Functional site 1) chain A residue 104 type sequence V description binding site for residue PLM A 401 source : AC1 2) chain A residue 124 type sequence L description binding site for residue PLM A 401 source : AC1 3) chain A residue 126 type sequence H description binding site for residue PLM A 401 source : AC1 4) chain A residue 130 type sequence W description binding site for residue PLM A 401 source : AC1 5) chain A residue 164 type sequence R description binding site for residue PLM A 401 source : AC1 6) chain A residue 196 type sequence C description binding site for residue PLM A 401 source : AC1 7) chain A residue 255 type sequence D description binding site for residue MG A 402 source : AC2 8) chain A residue 257 type sequence S description binding site for residue MG A 402 source : AC2 9) chain B residue 104 type sequence V description binding site for residue PLM B 401 source : AC3 10) chain B residue 126 type sequence H description binding site for residue PLM B 401 source : AC3 11) chain B residue 130 type sequence W description binding site for residue PLM B 401 source : AC3 12) chain B residue 133 type sequence A description binding site for residue PLM B 401 source : AC3 13) chain B residue 146 type sequence T description binding site for residue PLM B 401 source : AC3 14) chain B residue 164 type sequence R description binding site for residue PLM B 401 source : AC3 15) chain B residue 196 type sequence C description binding site for residue PLM B 401 source : AC3 16) 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 17) 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 18) 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 19) 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 20) chain A residue 126 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 164 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 206 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 229 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 126 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 164 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 206 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 229 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3

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