eF-site ID 1y8p-AB PDB Code 1y8p Chain A, B click to enlarge Title Crystal structure of the PDK3-L2 complex Classification TRANSFERASE Compound [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3 Source Homo sapiens (Human) (ODP2_HUMAN) Sequence A:  VPKQIERYSRFSPSPLSIKQFLDFGRDNACEKTSYMFLRK ELPVRLANTMREVNLLPDNLLNRPSVGLVQSWYMQSFLEL LEYENKSPEDPQVLDNFLQVLIKVRNRHNDVVPTMAQGVI EYKEKFGFDPFISTNIQYFLDRFYTNRISFRMLINQHTLL FGGDTNPVHPKHIGSIDPTCNVADVVKDAYETAKMLCEQY YLVAPELEVEEFNAKAPDKPIQVVYVPSHLFHMLFELFKN SMRATVELYEDRKEGYPAVKTLVTLGKEDLSIKISDLGGG VPLRKIDRLFNYMYSTAPRPLAGFGYGLPISRLYARYFQG DLKLYSMEGVGTDAVIYLKALSSESFERLPVFNKSAWRHY KTTPEADDWSNPSSEPRDASK B:  SYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLA EIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCII VEKEADISAFADYTDLK Description Functional site 1) chain A residue 251 type sequence N description BINDING SITE FOR RESIDUE MG A 501 source : AC1 2) chain A residue 20 type sequence S description BINDING SITE FOR RESIDUE K A 502 source : AC2 3) chain A residue 21 type sequence R description BINDING SITE FOR RESIDUE K A 502 source : AC2 4) chain A residue 22 type sequence F description BINDING SITE FOR RESIDUE K A 502 source : AC2 5) chain A residue 59 type sequence N description BINDING SITE FOR RESIDUE K A 502 source : AC2 6) chain A residue 372 type sequence F description BINDING SITE FOR RESIDUE K A 502 source : AC2 7) chain A residue 300 type sequence L description BINDING SITE FOR RESIDUE K A 503 source : AC3 8) chain A residue 302 type sequence N description BINDING SITE FOR RESIDUE K A 503 source : AC3 9) chain A residue 305 type sequence Y description BINDING SITE FOR RESIDUE K A 503 source : AC3 10) chain A residue 325 type sequence G description BINDING SITE FOR RESIDUE K A 503 source : AC3 11) chain A residue 45 type sequence S description BINDING SITE FOR RESIDUE RED B 373 source : AC4 12) chain A residue 48 type sequence F description BINDING SITE FOR RESIDUE RED B 373 source : AC4 13) chain B residue 173 type sequence K description BINDING SITE FOR RESIDUE RED B 373 source : AC4 14) chain A residue 247 type sequence E description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 15) chain A residue 250 type sequence K description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 16) chain A residue 251 type sequence N description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 17) chain A residue 254 type sequence R description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 18) chain A residue 255 type sequence A description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 19) chain A residue 287 type sequence D description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 20) chain A residue 292 type sequence V description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 21) chain A residue 300 type sequence L description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 22) chain A residue 305 type sequence Y description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 23) chain A residue 306 type sequence S description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 24) chain A residue 307 type sequence T description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 25) chain A residue 321 type sequence L description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 26) chain A residue 322 type sequence A description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 27) chain A residue 323 type sequence G description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 28) chain A residue 324 type sequence F description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 29) chain A residue 325 type sequence G description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 30) chain A residue 326 type sequence Y description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 31) chain A residue 327 type sequence G description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 32) chain A residue 328 type sequence L description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 33) chain A residue 352 type sequence T description BINDING SITE FOR RESIDUE ATP A 504 source : AC5 34) chain A residue 278 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q922H2 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 138-149 type prosite sequence PALSPTMTMGTV description AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PalSPtMTMGTV source prosite : PS00178 36) chain B residue 157-186 type prosite sequence GEKLSEGDLLAEIETDKATIGFEVQEEGYL description LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GekLsegDLLaeIETdKATigFevqeeGyL source prosite : PS00189 37) chain B residue 206 type MOD_RES sequence I description N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:25525879, ECO:0007744|PDB:1Y8N, ECO:0007744|PDB:1Y8O, ECO:0007744|PDB:1Y8P, ECO:0007744|PDB:2PNR, ECO:0007744|PDB:2Q8I source Swiss-Prot : SWS_FT_FI1 38) chain A residue 287 type MOD_RES sequence D description N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:25525879, ECO:0007744|PDB:1Y8N, ECO:0007744|PDB:1Y8O, ECO:0007744|PDB:1Y8P, ECO:0007744|PDB:2PNR, ECO:0007744|PDB:2Q8I source Swiss-Prot : SWS_FT_FI1 39) chain A residue 306 type MOD_RES sequence S description N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:25525879, ECO:0007744|PDB:1Y8N, ECO:0007744|PDB:1Y8O, ECO:0007744|PDB:1Y8P, ECO:0007744|PDB:2PNR, ECO:0007744|PDB:2Q8I source Swiss-Prot : SWS_FT_FI1 40) chain A residue 323 type MOD_RES sequence G description N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:25525879, ECO:0007744|PDB:1Y8N, ECO:0007744|PDB:1Y8O, ECO:0007744|PDB:1Y8P, ECO:0007744|PDB:2PNR, ECO:0007744|PDB:2Q8I source Swiss-Prot : SWS_FT_FI1

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