Structure of PDB 3ael Chain D

Receptor sequence
>3aelD (length=384) Species: 5759 (Entamoeba histolytica) [Search protein sequence]
DITTTLLHPKGDHVLHSHAYPIFQTSTFCFDSTQQGADLFMGKGEGHIYS
RLGNPTVEQFEEMVCSIEGAAGSAAFGSGMGAISSSTLAFLQKGDHLIAG
DTLYGCTVSLFTHWLPRFGIEVDLIDTSDVEKVKAAWKPNTKMVYLESPA
NPTCKVSDIKGIAVVCHERGARLVVDATFTSPCFLKPLELGADIALHSVS
KYINGHGDVIGGVSSAKTAEDIATIKFYRKDAGSLMAPMDAFLCARGMKT
LPIRMQIHMENGLKVAKFLEQHEKIVKVNHPGLESFPGHDIAKKQMTGYG
STFLFEMKSFEAAKKLMEHLKVCTLAVSLGCVDTLIEHPASMTHAAVPEN
IMRKQGITPELVRISVGIENVDDIIADLKQALEL
3D structure
PDB3ael Crystal structure of Entamoeba histolytica methionine gamma-lyase 1
ChainD
Resolution2.0 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 4LM D Y1553 R1555 Y49 R51
BS02 2LM D G1583 M1584 Y1608 N1655 D1680 T1682 S1702 S1704 K1705 V1831 S1832 T1847 R1867 G79 M80 Y104 N151 D176 T178 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:3ael, PDBe:3ael, PDBj:3ael
PDBsum3ael
PubMed
UniProtQ86D28

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