eF-site ID 3b7w-A PDB Code 3b7w Chain A click to enlarge Title Crystal structure of human acyl-CoA synthetase medium-chain family member 2A, with L64P mutation Classification LIGASE Compound Acyl-coenzyme A synthetase ACSM2A, mitochondrial precursor Source Homo sapiens (Human) (ACS2A_HUMAN) Sequence A:  LQWGHQEVPAKFNFASDVLDHWADMEKAGKRPPSPALWWV NGKGKELMWNFRELSENSQQAANVLSGACGLQRGDRVAVV LPRVPEWWLVILGCIRAGLIFMPGTIQMKSTDILYRLQMS KAKAIVAGDEVIQEVDTVASECPSLRIKLLVSEKSCDGWL NFKKLLNEASTTHHCVETGSQEASAIYFTSGTSGLPKMAE HSYSSLGLKAKMDAGWTGLQASDIMWTISDTGWILNILCS LMEPWALGACTFVHLLPKFDPLVILKTLSSYPIKSMMGAP IVYRMLLQQDLSSYKFPHLQNCVTVGESLLPETLENWRAQ TGLDIRESYGQTETGLTCMVSKTMKIKPGYMGTAASCYDV QIIDDKGNVLPPGTEGDIGIRVKPIRPIGIFSGYVDNPDK TAANIRGDFWLLGDRGIKDEDGYFQFMGRADDIINSSGYR IGPSEVENALMEHPAVVETAVISSPDPVRGEVVKAFVVLA SQFLSHDPEQLTKELQQHVKSVTAPYKYPRKIEFVLNLPK TVTGKIQRAKLRDKEWK Description Functional site 1) chain A residue 483 type sequence M description BINDING SITE FOR RESIDUE MG A 601 source : AC1 2) chain A residue 485 type sequence H description BINDING SITE FOR RESIDUE MG A 601 source : AC1 3) chain A residue 488 type sequence V description BINDING SITE FOR RESIDUE MG A 601 source : AC1 4) chain A residue 472 type sequence R description BINDING SITE FOR RESIDUE CL A 602 source : AC2 5) chain A residue 345 type sequence T description BINDING SITE FOR RESIDUE CL A 603 source : AC3 6) chain A residue 348 type sequence N description BINDING SITE FOR RESIDUE CL A 603 source : AC3 7) chain A residue 352 type sequence Q description BINDING SITE FOR RESIDUE CL A 604 source : AC4 8) chain A residue 301 type sequence S description BINDING SITE FOR RESIDUE CL A 605 source : AC5 9) chain A residue 302 type sequence S description BINDING SITE FOR RESIDUE CL A 605 source : AC5 10) chain A residue 301 type sequence S description BINDING SITE FOR RESIDUE GOL A 606 source : AC6 11) chain A residue 302 type sequence S description BINDING SITE FOR RESIDUE GOL A 606 source : AC6 12) chain A residue 303 type sequence Y description BINDING SITE FOR RESIDUE GOL A 606 source : AC6 13) chain A residue 304 type sequence P description BINDING SITE FOR RESIDUE GOL A 606 source : AC6 14) chain A residue 399 type sequence G description BINDING SITE FOR RESIDUE GOL A 606 source : AC6 15) chain A residue 400 type sequence N description BINDING SITE FOR RESIDUE GOL A 606 source : AC6 16) chain A residue 401 type sequence V description BINDING SITE FOR RESIDUE GOL A 606 source : AC6 17) chain A residue 413 type sequence R description BINDING SITE FOR RESIDUE GOL A 606 source : AC6 18) chain A residue 440 type sequence D description BINDING SITE FOR RESIDUE GOL A 606 source : AC6 19) chain A residue 513 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q68CK6 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 218-229 type prosite sequence IYFTSGTSGLPK description AMP_BINDING Putative AMP-binding domain signature. IYFTSGTSGlPK source prosite : PS00455 21) chain A residue 139 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:19345228 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 364 type BINDING sequence T description BINDING => ECO:0000269|PubMed:19345228 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 469 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19345228 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 472 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19345228 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19345228 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 532 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19345228 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 540 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19345228 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 221 type BINDING sequence T description BINDING => ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 359 type BINDING sequence E description BINDING => ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 446 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 461 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 557 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7 source Swiss-Prot : SWS_FT_FI2

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