Structure of PDB 1e5e Chain B

Receptor sequence
>1e5eB (length=393) Species: 412133 (Trichomonas vaginalis G3) [Search protein sequence]
ERMTPATACIHANPQKDQFGAAIPPIYQTSTFVFDNCQQGGNRFAGQESG
YIYTRLGNPTVSNLEGKIAFLEKTEACVATSSGMGAIAATVLTILKAGDH
LISDECLYGCTHALFEHALTKFGIQVDFINTAIPGEVKKHMKPNTKIVYF
ETPANPTLKIIDMERVCKDAHSQEGVLVIADNTFCSPMITNPVDFGVDVV
VHSATKYINGHTDVVAGLICGKADLLQQIRMVGIKDITGSVISPHDAWLI
TRGLSTLNIRMKAESENAMKVAEYLKSHPAVEKVYYPGFEDHEGHDIAKK
QMRMYGSMITFILKSGFEGAKKLLDNLKLITLAVSLGGCESLIQHPASMT
HAVVPKEEREAAGITDGMIRLSVGIEDADELIADFKQGLDALL
3D structure
PDB1e5e The Primitive Protozoon Trichomonas Vaginalis Contains Two Methionine Gamma-Lyase Genes that Encode Members of the Gamma Family of Pyridoxal 5'-Phosphate Enzymes
ChainB
Resolution2.18 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R58 Y111 D184 K209
Catalytic site (residue number reindexed from 1) R55 Y108 D181 K206
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 PPJ B Y56 R58 Y53 R55
BS02 PPJ B G86 M87 Y111 N158 D184 S206 T208 K209 S338 T353 R373 G83 M84 Y108 N155 D181 S203 T205 K206 S335 T350 R370
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:1e5e, PDBe:1e5e, PDBj:1e5e
PDBsum1e5e
PubMed
UniProtA2FEV4

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