Structure of PDB 3aeo Chain D

Receptor sequence
>3aeoD (length=384) Species: 5759 (Entamoeba histolytica) [Search protein sequence]
DITTTLLHPKGDHVLHSHAYPIFQTSTFCFDSTQQGADLFMGKGEGHIYS
RLGNPTVEQFEEMVCSIEGAAGSAAFGSGMGAISSSTLAFLQKGDHLIAG
DTLYGCTVSLFTHWLPRFGIEVDLIDTSDVEKVKAAWKPNTKMVYLESPA
NPTCKVSDIKGIAVVCHERGARLVVDATFTSPCFLKPLELGADIALHSVS
KYINGHGDVIGGVSSAKTAEDIATIKFYRKDAGSLMAPMDAFLCARGMKT
LPIRMQIHMENGLKVAKFLEQHEKIVKVNHPGLESFPGHDIAKKQMTGYG
STFLFEMKSFEAAKKLMEHLKVCTLAVSLGCVDTLIEHPASMTHAAVPEN
IMRKQGITPELVRISVGIENVDDIIADLKQALEL
3D structure
PDB3aeo Crystal structure of Entamoeba histolytica methionine gamma-lyase 1
ChainD
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R1555 Y1608 D1680 K1705
Catalytic site (residue number reindexed from 1) R51 Y104 D176 K201
Enzyme Commision number 4.4.1.11: methionine gamma-lyase.
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 Y1553 R1555 Y49 R51
BS02 3LM D G1583 M1584 Y1608 N1655 D1680 S1702 S1704 K1705 V1831 S1832 T1847 R1867 G79 M80 Y104 N151 D176 S198 S200 K201 V327 S328 T343 R363
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
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:3aeo, PDBe:3aeo, PDBj:3aeo
PDBsum3aeo
PubMed
UniProtQ86D28

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