Structure of PDB 5x2w Chain A

Receptor sequence
>5x2wA (length=392) Species: 303 (Pseudomonas putida) [Search protein sequence]
LPGFATRAIHHGYDPQDHGGALVPPVYQTATFTFPTVEYGAACFAGEQAG
HFYSRISNPTLNLLEARMASLEGGEAGLALASGMGAITSTLWTLLRPGDE
VLLGNTLYGCTFAFLHHGIGEFGVKLRHVDMADLQALEAAMTPATRVIYF
ESPANPNMHMADIAGVAKIARKHGATVVVDNTYCTPYLQRPLELGADLVV
HSATKYLSGHGDITAGIVVGSQALVDRIRLQGLKDMTGAVLSPHDAALLM
RGIKTLNLRMDRHCANAQVLAEFLARQPQVELIHYPGLASFPQYTLARQQ
MSQPGGMIAFELKGGIGAGRRFMNALQLFSRAVSLGDAESLAQHPASMTH
SSYTPEERAHYGISEGLVRLSVGLEDIDDLLADVQQALKASA
3D structure
PDB5x2w Structural and mechanistic insights into homocysteine degradation by a mutant of methionine gamma-lyase based on substrate-assisted catalysis
ChainA
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) R55 Y108 D180 K205
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 A S88 G89 M90 Y114 D186 S208 K211 V339 S340 R375 S82 G83 M84 Y108 D180 S202 K205 V333 S334 R369
BS02 3LM A Y59 R61 Y53 R55
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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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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