Structure of PDB 4oma Chain A

Receptor sequence
>4omaA (length=396) Species: 546 (Citrobacter freundii) [Search protein sequence]
SDCRTYGFNTQIVHAGQQPDPSTGALSTPIFQTSTFVFDSAEQGAARFAL
EESGYIYTRLGNPTTDALEKKLAVLERGEAGLATASGISAITTTLLTLCQ
QGDHIVSASAIYGCTHAFLSHSMPKFGINVSFVDAAKPEEIRAAMRPETK
VVYIETPANPTLSLVDIETVAGIAHQQGALLVVDNTFMSPYCQQPLQLGA
DIVVHSVTKYINGHGDVIGGIIVGKQEFIDQARFVGLKDITGGCMSPFNA
WLTLRGVKTLGIRMERHCENALKIARFLEGHPSITRVYYPGLSSHPQYEL
GQRQMSLPGGIISFEIAGGLEAGRRMINSVELCLLAVSLGDTETLIQHPA
SMTHSPVAPEERLKAGITDGLIRLSVGLEDPEDIINDLEHAIRKAT
3D structure
PDB4oma Pre-steady-state Kinetic and Structural Analysis of Interaction of Methionine gamma-Lyase from Citrobacter freundii with Inhibitors.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R60 Y113 D185 K210
Catalytic site (residue number reindexed from 1) R59 Y112 D184 K209
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 LCS A G88 I89 Y113 D185 S207 T209 K210 V338 S339 R374 G87 I88 Y112 D184 S206 T208 K209 V337 S338 R373 PDBbind-CN: -logKd/Ki=4.17,Ki=68uM
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:4oma, PDBe:4oma, PDBj:4oma
PDBsum4oma
PubMed25398880
UniProtQ84AR1

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