eF-site ID 5f34-C PDB Code 5f34 Chain C 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 C:  PEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFR LPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGN WDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGF EVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQ VDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMR VYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQ WIADLSDERRAR Description Functional site 1) chain C residue 124 type sequence L description binding site for residue HD6 C 401 source : AC3 2) chain C residue 130 type sequence W description binding site for residue HD6 C 401 source : AC3 3) chain C residue 133 type sequence A description binding site for residue HD6 C 401 source : AC3 4) chain C residue 134 type sequence G description binding site for residue HD6 C 401 source : AC3 5) chain C residue 196 type sequence C description binding site for residue HD6 C 401 source : AC3 6) chain C residue 198 type sequence M description binding site for residue HD6 C 401 source : AC3 7) chain C residue 202 type sequence D description binding site for residue HD6 C 401 source : AC3 8) chain C residue 220 type sequence P description binding site for residue HD6 C 401 source : AC3 9) chain C residue 222 type sequence G description binding site for residue HD6 C 401 source : AC3 10) chain C residue 126 type BINDING sequence H description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 11) chain C residue 164 type BINDING sequence R description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 12) chain C residue 206 type BINDING sequence S description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 13) chain C residue 229 type BINDING sequence E description BINDING => ECO:0000305|PubMed:26965057 source Swiss-Prot : SWS_FT_FI3 14) 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 15) 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

Display surface Download Links