Structure of PDB 5x2w Chain D

Receptor sequence
>5x2wD (length=398) Species: 303 (Pseudomonas putida) [Search protein sequence]
MHGSNKLPGFATRAIHHGYDPQDHGGALVPPVYQTATFTFPTVEYGAACF
AGEQAGHFYSRISNPTLNLLEARMASLEGGEAGLALASGMGAITSTLWTL
LRPGDEVLLGNTLYGCTFAFLHHGIGEFGVKLRHVDMADLQALEAAMTPA
TRVIYFESPANPNMHMADIAGVAKIARKHGATVVVDNTYCTPYLQRPLEL
GADLVVHSATKYLSGHGDITAGIVVGSQALVDRIRLQGLKDMTGAVLSPH
DAALLMRGIKTLNLRMDRHCANAQVLAEFLARQPQVELIHYPGLASFPQY
TLARQQMSQPGGMIAFELKGGIGAGRRFMNALQLFSRAVSLGDAESLAQH
PASMTHSSYTPEERAHYGISEGLVRLSVGLEDIDDLLADVQQALKASA
3D structure
PDB5x2w Structural and mechanistic insights into homocysteine degradation by a mutant of methionine gamma-lyase based on substrate-assisted catalysis
ChainD
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R61 Y114 D186 K211
Catalytic site (residue number reindexed from 1) R61 Y114 D186 K211
Enzyme Commision number 4.4.1.11: methionine gamma-lyase.
4.4.1.2: homocysteine desulfhydrase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 3LM D Y59 R61 Y59 R61
BS02 3LM D G89 M90 Y114 N161 D186 S208 K211 V339 R375 G89 M90 Y114 N161 D186 S208 K211 V339 R375
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0016846 carbon-sulfur lyase activity
GO:0018826 methionine gamma-lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0047982 homocysteine desulfhydrase activity
Biological Process
GO:0019346 transsulfuration
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5x2w, PDBe:5x2w, PDBj:5x2w
PDBsum5x2w
PubMed28329912
UniProtP13254|MEGL_PSEPU L-methionine gamma-lyase (Gene Name=mdeA)

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