Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T06397 | Target Info | |||
| Target Name | Pseudomonas Methionine gamma-lyase (Pseudo mdeA) | ||||
| Synonyms | Pseudo MGL; L-methionine gamma-lyase; L-methioninase; Homocysteine desulfhydrase | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | Pseudo mdeA | ||||
| Biochemical Class | Carbon-sulfur lyases | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | L-methionine | Ligand Info | |||
| Canonical SMILES | CSCCC(C(=O)O)N | ||||
| InChI | 1S/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1 | ||||
| InChIKey | FFEARJCKVFRZRR-BYPYZUCNSA-N | ||||
| PubChem Compound ID | 6137 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 3VK3 Crystal Structure of L-Methionine gamma-Lyase from Pseudomonas putida C116H Mutant Complexed with L-methionine | ||||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | Yes | [1] |
| PDB Sequence |
HGSNKLPGFA
11 TRAIHHGYDP21 QDHGGALVPP31 VYQTATFTFP41 TVEYGAACFA51 GEQAGHFYSR 61 ISNPTLNLLE71 ARMASLEGGE81 AGLALASGMG91 AITSTLWTLL101 RPGDEVLLGN 111 TLYGHTFAFL121 HHGIGEFGVK131 LRHVDMADLQ141 ALEAAMTPAT151 RVIYFESPAN 161 PNMHMADIAG171 VAKIARKHGA181 TVVVDNTYCT191 PYLQRPLELG201 ADLVVHSATY 212 LSGHGDITAG222 IVVGSQALVD232 RIRLQGLKDM242 TGAVLSPHDA252 ALLMRGIKTL 262 NLRMDRHCAN272 AQVLAEFLAR282 QPQVELIHYP292 GLASFPQYTL302 ARQQMSQPGG 312 MIAFELKGGI322 GAGRRFMNAL332 QLFSRAVSLG342 DAESLAQHPA352 SMTHSSYTPE 362 ERAHYGISEG372 LVRLSVGLED382 IDDLLADVQQ392 ALKASA
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| PDB ID: 7F1U Crystal structure of Pseudomonas putida methionine gamma-lyase Q349S mutant with L-methionine intermediates | ||||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | Yes | [2] |
| PDB Sequence |
> Chain A
GSNKLPGFAT 12 RAIHHGYDPQ22 DHGGALVPPV32 YQTATFTFPT42 VEYGAACFAG52 EQAGHFYSRI 62 SNPTLNLLEA72 RMASLEGGEA82 GLALASGMGA92 ITSTLWTLLR102 PGDEVLLGNT 112 LYGCTFAFLH122 HGIGEFGVKL132 RHVDMADLQA142 LEAAMTPATR152 VIYFESPANP 162 NMHMADIAGV172 AKIARKHGAT182 VVVDNTYCTP192 YLQRPLELGA202 DLVVHSATKY 212 LSGHGDITAG222 IVVGSQALVD232 RIRLQGLKDM242 TGAVLSPHDA252 ALLMRGIKTL 262 NLRMDRHCAN272 AQVLAEFLAR282 QPQVELIHYP292 GLASFPQYTL302 ARQQMSQPGG 312 MIAFELKGGI322 GAGRRFMNAL332 QLFSRAVSLG342 DAESLASHPA352 SMTHSSYTPE 362 ERAHYGISEG372 LVRLSVGLED382 IDDLLADVQQ392 ALKASA> Chain B LPGFATRAIH 16 HGYDPQDHGG26 ALVPPVYQTA36 TFTFPTVEYG46 AACFAGEQAG56 HFYSRISNPT 66 LNLLEARMAS76 LEGGEAGLAL86 ASGMGAITST96 LWTLLRPGDE106 VLLGNTLYGC 116 TFAFLHHGIG126 EFGVKLRHVD136 MADLQALEAA146 MTPATRVIYF156 ESPANPNMHM 166 ADIAGVAKIA176 RKHGATVVVD186 NTYCTPYLQR196 PLELGADLVV206 HSATYLSGHG 217 DITAGIVVGS227 QALVDRIRLQ237 GLKDMTGAVL247 SPHDAALLMR257 GIKTLNLRMD 267 RHCANAQVLA277 EFLARQPQVE287 LIHYPGLASF297 PQYTLARQQM307 SQPGGMIAFE 317 LKGGIGAGRR327 FMNALQLFSR337 AVSLGDAESL347 ASHPASMTHS357 SYTPEERAHY 367 GISEGLVRLS377 VGLEDIDDLL387 ADVQQALKAS397 A
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | The role of amino acid residues in the active site of L-methionine Gamma-lyase from Pseudomonas putida. Biosci Biotechnol Biochem. 2012;76(7):1275-84. | ||||
| REF 2 | Characterization and application of l-methionine Gamma-lyase Q349S mutant enzyme with an enhanced activity toward l-homocysteine. J Biosci Bioeng. 2022 Mar;133(3):213-221. | ||||
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