eF-site ID 4u0o-B PDB Code 4u0o Chain B click to enlarge Title Crystal structure of Thermosynechococcus elongatus Lipoyl Synthase 2 complexed with MTA and DTT Classification TRANSFERASE Compound Lipoyl synthase 2 Source Thermosynechococcus elongatus (strain BP-1) (LIPA2_THEEB) Sequence B:  PSWLRISTVQRLVRQYGIHTICEEGRCPNRGECYGQKTAT FLLLGPTCTRACAFCQVEKGHAPAAVDPEEPTKIAAAVAT LGLRYVVLTSVARDDLPDQGAGQFVATMAAIRQRCPGTEI EVLSPDFRMDRGRLSQRDCIAQIVAAQPACYNHNLETVRR LQGPVRRGATYESSLRVLATVKELNPDIPTKSGLMLGLGE TEAEIIETLKDLRRVGCDRLTLGQYLPPSLSHLPVVKYWT PEEFNTLGNIARELGFSHVRSGPLVRSSYHAAE Description Functional site 1) chain B residue 63 type sequence C description binding site for residue SF4 B 301 source : AC1 2) chain B residue 67 type sequence C description binding site for residue SF4 B 301 source : AC1 3) chain B residue 69 type sequence F description binding site for residue SF4 B 301 source : AC1 4) chain B residue 70 type sequence C description binding site for residue SF4 B 301 source : AC1 5) chain B residue 37 type sequence C description binding site for residue SF4 B 302 source : AC2 6) chain B residue 42 type sequence C description binding site for residue SF4 B 302 source : AC2 7) chain B residue 44 type sequence N description binding site for residue SF4 B 302 source : AC2 8) chain B residue 48 type sequence C description binding site for residue SF4 B 302 source : AC2 9) chain B residue 55 type sequence T description binding site for residue SF4 B 302 source : AC2 10) chain B residue 283 type sequence S description binding site for residue SF4 B 302 source : AC2 11) chain B residue 36 type sequence I description binding site for residue DTT B 303 source : AC3 12) chain B residue 104 type sequence T description binding site for residue DTT B 303 source : AC3 13) chain B residue 105 type sequence S description binding site for residue DTT B 303 source : AC3 14) chain B residue 69 type sequence F description binding site for residue MTA B 304 source : AC4 15) chain B residue 169 type sequence N description binding site for residue MTA B 304 source : AC4 16) chain B residue 171 type sequence E description binding site for residue MTA B 304 source : AC4 17) chain B residue 210 type sequence M description binding site for residue MTA B 304 source : AC4 18) chain B residue 239 type sequence Q description binding site for residue MTA B 304 source : AC4 19) chain B residue 241 type sequence L description binding site for residue MTA B 304 source : AC4 20) chain B residue 281 type sequence R description binding site for residue MTA B 304 source : AC4 21) chain B residue 283 type sequence S description binding site for residue MTA B 304 source : AC4 22) chain B residue 63 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O, ECO:0007744|PDB:4U0P source Swiss-Prot : SWS_FT_FI1 23) chain B residue 67 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O, ECO:0007744|PDB:4U0P source Swiss-Prot : SWS_FT_FI1 24) chain B residue 70 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O, ECO:0007744|PDB:4U0P source Swiss-Prot : SWS_FT_FI1 25) chain B residue 37 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O, ECO:0007744|PDB:4U0P source Swiss-Prot : SWS_FT_FI1 26) chain B residue 42 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O, ECO:0007744|PDB:4U0P source Swiss-Prot : SWS_FT_FI1 27) chain B residue 48 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O, ECO:0007744|PDB:4U0P source Swiss-Prot : SWS_FT_FI1 28) chain B residue 283 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O source Swiss-Prot : SWS_FT_FI2

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