Target Binding Site Detail
Target General Information | Top | ||||
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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 | ||||
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Ligand Name | Hydrogen Sulfide | Ligand Info | |||
Canonical SMILES | S | ||||
InChI | 1S/H2S/h1H2 | ||||
InChIKey | RWSOTUBLDIXVET-UHFFFAOYSA-N | ||||
PubChem Compound ID | 402 |
Drug Binding Sites of Target | Top | |||||
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PDB ID: 5X30 Crystal structure of Pseudomonas putida methionine gamma-lyase C116H mutant with L-homocysteine intermediates. | ||||||
Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | Yes | [1] |
PDB Sequence |
> Chain A
LPGFATRAIH 16 HGYDPQDHGG26 ALVPPVYQTA36 TFTFPTVEYG46 AACFAGEQAG56 HFYSRISNPT 66 LNLLEARMAS76 LEGGEAGLAL86 ASGMGAITST96 LWTLLRPGDE106 VLLGNTLYGH 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 AQHPASMTHS357 SYTPEERAHY 367 GISEGLVRLS377 VGLEDIDDLL387 ADVQQALKAS397 A> Chain B LPGFATRAIH 16 HGYDPQDHGG26 ALVPPVYQTA36 TFTFPTVEYG46 AACFAGEQAG56 HFYSRISNPT 66 LNLLEARMAS76 LEGGEAGLAL86 ASGMGAITST96 LWTLLRPGDE106 VLLGNTLYGH 116 TFAFLHHGIG126 EFGVKLRHVD136 MADLQALEAA146 MTPATRVIYF156 ESPANPNMHM 166 ADIAGVAKIA176 RKHGATVVVD186 NTYCTPYLQR196 PLELGADLVV206 HSATKYLSGH 216 GDITAGIVVG226 SQALVDRIRL236 QGLKDMTGAV246 LSPHDAALLM256 RGIKTLNLRM 266 DRHCANAQVL276 AEFLARQPQV286 ELIHYPGLAS296 FPQYTLARQQ306 MSQPGGMIAF 316 ELKGGIGAGR326 RFMNALQLFS336 RAVSLGDAES346 LAQHPASMTH356 SSYTPEERAH 366 YGISEGLVRL376 SVGLEDIDDL386 LADVQQALKA396 SA
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PDB ID: 5X2X Crystal structure of Pseudomonas putida methionine gamma-lyase wild type with L-homocysteine intermediates | ||||||
Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] |
PDB Sequence |
LPGFATRAIH
16 HGYDPQDHGG26 ALVPPVYQTA36 TFTFPTVEYG46 AACFAGEQAG56 HFYSRISNPT 66 LNLLEARMAS76 LEGGEAGLAL86 ASGMGAITST96 LWTLLRPGDE106 VLLGNTLYGC 116 TFAFLHHGIG126 EFGVKLRHVD136 MADLQALEAA146 MTPATRVIYF156 ESPANPNMHM 166 ADIAGVAKIA176 RKHGATVVVD186 NTYCTPYLQR196 PLELGADLVV206 HSATKYLSGH 216 GDITAGIVVG226 SQALVDRIRL236 QGLKDMTGAV246 LSPHDAALLM256 RGIKTLNLRM 266 DRHCANAQVL276 AEFLARQPQV286 ELIHYPGLAS296 FPQYTLARQQ306 MSQPGGMIAF 316 ELKGGIGAGR326 RFMNALQLFS336 RAVSLGDAES346 LAQHPASMTH356 SSYTPEERAH 366 YGISEGLVRL376 SVGLEDIDDL386 LADVQQALKA396 SA
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References | Top | ||||
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REF 1 | Structural and mechanistic insights into homocysteine degradation by a mutant of methionine Gamma-lyase based on substrate-assisted catalysis. Protein Sci. 2017 Jun;26(6):1224-1230. |
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