eF-site ID 1dgd-A PDB Code 1dgd Chain A click to enlarge Title AN ALKALI METAL ION SIZE-DEPENDENT SWITCH IN THE ACTIVE SITE STRUCTURE OF DIALKYLGLYCINE DECARBOXYLASE Classification LYASE Compound DIALKYLGLYCINE DECARBOXYLASE Source Burkholderia cepacia (Pseudomonas cepacia) (DGDA_BURCE) Sequence A:  LNDDATFWRNARHHLVRYGGTFEPMIIERAKGSFVYDADG RAILDFTSGQMSAVLGHCHPEIVSVIGEYAGKLDHLFSGM LSRPVVDLATRLANITPPGLDRALLLSTGAESNEAAIRMA KLVTGKYEIVGFAQSWHGMTGAAASATYSAGRKGVGPAAV GSFAIPAPFTYRPRFERNGAYDYLAELDYAFDLIDRQSSG NLAAFIAEPILSSGGIIELPDGYMAALKRKCEARGMLLIL DEAQTGVGRTGTMFACQRDGVTPDILTLSKTLGAGLPLAA IVTSAAIEERAHELGYLFYTTHVSDPLPAAVGLRVLDVVQ RDGLVARANVMGDRLRRGLLDLMERFDCIGDVRGRGLLLG VEIVKDRRTKEPADGLGAKITRECMNLGLSMNIVQLPGMG GVFRIAPPLTVSEDEIDLGLSLLGQAIERAL Description (1)  DIALKYLGLYCINE DECARBOXYLASE (PYRUVATE) (DGD) (E.C.4.1.1.64) MUTANT WITH GLN 15 REPLACED BY HIS (Q15H) COMPLEXED WITH LITHIUM+ IN METAL-BINDING SITE 1 Functional site 1) chain A residue 52 type sequence Q description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 2) chain A residue 53 type sequence M description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 3) chain A residue 79 type sequence F description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 4) chain A residue 110 type sequence T description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 5) chain A residue 111 type sequence G description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 6) chain A residue 115 type sequence N description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 7) chain A residue 137 type sequence S description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 8) chain A residue 138 type sequence W description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 9) chain A residue 141 type sequence M description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 10) chain A residue 210 type sequence E description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 11) chain A residue 214 type sequence S description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 12) chain A residue 215 type sequence S description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 13) chain A residue 243 type sequence D description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 14) chain A residue 245 type sequence A description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 15) chain A residue 246 type sequence Q description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 16) chain A residue 272 type sequence K description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 17) chain A residue 301 type sequence Y description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 18) chain A residue 303 type sequence T description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 19) chain A residue 394 type sequence N description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 20) chain A residue 406 type sequence R description ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND source : ACT 21) chain A residue 78 type sequence L description METAL BINDING SITE 1 (NEAR THE ACTIVE SITE): LIGANDS TO THE LI+ ION ARE INDICATED source : ME1 22) chain A residue 307 type sequence D description METAL BINDING SITE 1 (NEAR THE ACTIVE SITE): LIGANDS TO THE LI+ ION ARE INDICATED source : ME1 23) chain A residue 95 type sequence A description METAL BINDING SITE 2: LIGANDS TO THE NA+ ION ARE INDICATED source : ME2 24) chain A residue 98 type sequence T description METAL BINDING SITE 2: LIGANDS TO THE NA+ ION ARE INDICATED source : ME2 25) chain A residue 99 type sequence P description METAL BINDING SITE 2: LIGANDS TO THE NA+ ION ARE INDICATED source : ME2 26) chain A residue 102 type sequence L description METAL BINDING SITE 2: LIGANDS TO THE NA+ ION ARE INDICATED source : ME2 27) chain A residue 95 type sequence A description BINDING SITE FOR RESIDUE NA A 435 source : AC1 28) chain A residue 98 type sequence T description BINDING SITE FOR RESIDUE NA A 435 source : AC1 29) chain A residue 99 type sequence P description BINDING SITE FOR RESIDUE NA A 435 source : AC1 30) chain A residue 102 type sequence L description BINDING SITE FOR RESIDUE NA A 435 source : AC1 31) chain A residue 110 type sequence T description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 32) chain A residue 111 type sequence G description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 33) chain A residue 112 type sequence A description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 34) chain A residue 115 type sequence N description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 35) chain A residue 138 type sequence W description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 36) chain A residue 139 type sequence H description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 37) chain A residue 210 type sequence E description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 38) chain A residue 243 type sequence D description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 39) chain A residue 245 type sequence A description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 40) chain A residue 246 type sequence Q description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 41) chain A residue 272 type sequence K description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 42) chain A residue 302 type sequence T description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 43) chain A residue 303 type sequence T description BINDING SITE FOR RESIDUE PLP A 437 source : AC2 44) chain A residue 52 type sequence Q description BINDING SITE FOR RESIDUE MES A 434 source : AC3 45) chain A residue 138 type sequence W description BINDING SITE FOR RESIDUE MES A 434 source : AC3 46) chain A residue 152 type sequence A description BINDING SITE FOR RESIDUE MES A 434 source : AC3 47) chain A residue 215 type sequence S description BINDING SITE FOR RESIDUE MES A 434 source : AC3 48) chain A residue 246 type sequence Q description BINDING SITE FOR RESIDUE MES A 434 source : AC3 49) chain A residue 272 type sequence K description BINDING SITE FOR RESIDUE MES A 434 source : AC3 50) chain A residue 406 type sequence R description BINDING SITE FOR RESIDUE MES A 434 source : AC3 51) chain A residue 139 type catalytic sequence H description 482 source MCSA : MCSA1 52) chain A residue 211 type catalytic sequence P description 482 source MCSA : MCSA1 53) chain A residue 244 type catalytic sequence E description 482 source MCSA : MCSA1 54) chain A residue 247 type catalytic sequence T description 482 source MCSA : MCSA1 55) chain A residue 273 type catalytic sequence T description 482 source MCSA : MCSA1 56) chain A residue 407 type catalytic sequence I description 482 source MCSA : MCSA1 57) chain A residue 240-277 type prosite sequence LILDEAQTGVGRTGTMFACQRDGVTPDILTLSKTLGAG description AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIlDEAqt.GVgRtGtmfacqrdgvtp....DILtlSKtlgAG source prosite : PS00600 58) chain A residue 273 type MOD_RES sequence T description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI1

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