eF-site ID 2fw3-A PDB Code 2fw3 Chain A click to enlarge Title Crystal structure of rat carnitine palmitoyltransferase 2 in complex with antidiabetic drug ST1326 Classification TRANSFERASE Compound Carnitine O-palmitoyltransferase II, mitochondrial Source Rattus norvegicus (Rat) (CPT2_RAT) Sequence A:  DDYLQHSIVPTMHYQDSLPRLPIPKLEDTMKRYLNAQKPL LDDSQFRRTEALCKNFETGVGKELHAHLLAQDKQNKHTSY ISGPWFDMYLTARDSIVLNFNPFMAFNPDPKSEYNDQLTR ATNLTVSAVRFLKTLQAGLLEPEVFHLNPSKSDTDAFKRL IRFVPPSLSWYGAYLVNAYPLDMSQYFRLFNSTRIPRPNR DELFTDTKARHLLVLRKGHFYVFDVLDQDGNIVNPLEIQA HLKYILSDSSPVPEFPVAYLTSENRDVWAELRQKLIFDGN EETLKKVDSAVFCLCLDDFPMKDLIHLSHTMLHGDGTNRW FDKSFNLIVAEDGTAAVHFEHSWGDGVAVLRFFNEVFRDS TQTPAITPQSQPAATNSSASVETLSFNLSGALKAGITAAK EKFDTTVKTLSIDSIQFQRGGKEFLKKKQLSPDAVAQLAF QMAFLRQYGQTVATYESCSTAAFKHGRTETIRPASIFTKR CSEAFVRDPSKHSVGELQHMMAECSKYHGQLTKEAAMGQG FDRHLYALRYLATARGLNLPELYLDPAYQQMNHNILSTST LNSPAVSLGGFAPVVPDGFGIAYAVHDDWIGCNVSSYSGR NAREFLHCVQKCLEDIFDALEGK Description Functional site 1) chain A residue 372 type sequence H description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 2) chain A residue 447 type sequence Q description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 3) chain A residue 486 type sequence Y description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 4) chain A residue 488 type sequence S description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 5) chain A residue 499 type sequence T description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 6) chain A residue 588 type sequence S description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 7) chain A residue 590 type sequence S description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 8) chain A residue 602 type sequence F description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 9) chain A residue 605 type sequence V description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 10) chain A residue 613 type sequence A description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 11) chain A residue 622 type sequence G description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 12) chain A residue 623 type sequence C description BINDING SITE FOR RESIDUE BUI A 900 source : AC1 13) chain A residue 49-64 type prosite sequence LPRLPIPKLEDTMKRY description ACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPrLPIPkLeDTMkrY source prosite : PS00439 14) chain A residue 350-377 type prosite sequence RWFDKSFNLIVAEDGTAAVHFEHSWGDG description ACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWfDKsFnLIvaeDGtaavhfEHswgDG source prosite : PS00440 15) chain A residue 179-208 type INTRAMEM sequence NPSKSDTDAFKRLIRFVPPSLSWYGAYLVN description Note=Mitochondrial inner membrane source Swiss-Prot : SWS_FT_FI1 16) chain A residue 372 type ACT_SITE sequence H description Proton acceptor => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU source Swiss-Prot : SWS_FT_FI3 17) chain A residue 452 type BINDING sequence G description BINDING => ECO:0000269|PubMed:16615913, ECO:0007744|PDB:2DEB source Swiss-Prot : SWS_FT_FI4 18) chain A residue 486 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU source Swiss-Prot : SWS_FT_FI5 19) chain A residue 488 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU source Swiss-Prot : SWS_FT_FI5 20) chain A residue 499 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU source Swiss-Prot : SWS_FT_FI5 21) chain A residue 69 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52825 source Swiss-Prot : SWS_FT_FI6 22) chain A residue 85 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52825 source Swiss-Prot : SWS_FT_FI6 23) chain A residue 424 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52825 source Swiss-Prot : SWS_FT_FI6 24) chain A residue 439 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52825 source Swiss-Prot : SWS_FT_FI6 25) chain A residue 239 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52825 source Swiss-Prot : SWS_FT_FI7 26) chain A residue 510 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52825 source Swiss-Prot : SWS_FT_FI7 27) chain A residue 544 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52825 source Swiss-Prot : SWS_FT_FI7 28) chain A residue 305 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P52825 source Swiss-Prot : SWS_FT_FI8

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