Structure of PDB 5m3z Chain A

Receptor sequence
>5m3zA (length=395) Species: 546 (Citrobacter freundii) [Search protein sequence]
DCRTYGFNTQIVHAGQQPDPSTGALSTPIFQTSTFVFDSAEQGAARFALE
ESGYIYTRLGNPTTDALEKKLAVLERGEAGLATASGISAITTTLLTLCQQ
GDHIVSASAIYGHTHAFLSHSMPKFGINVSFVDAAKPEEIRAAMRPETKV
VYIETPANPTLSLVDIETVAGIAHQQGALLVVDNTFMSPYCQQPLQLGAD
IVVHSVTKYINGHGDVIGGIIVGKQEFIDQARFVGLKDITGGCMSPFNAW
LTLRGVKTLGIRMERHCENALKIARFLEGHPSITRVYYPGLSSHPQYELG
QRQMSLPGGIISFEIAGGLEAGRRMINSVELCLLAVSLGDTETLIQHPAS
MTHSPVAPEERLKAGITDGLIRLSVGLEDPEDIINDLEHAIRKAT
3D structure
PDB5m3z Crystal structure of mutant form Cys115His of Citrobacter freundii methionine gamma-lyase complexed with l-norleucine.
ChainA
Resolution1.45 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) R58 Y111 D183 K208
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 PLP A G88 I89 Y113 E156 D185 T187 S207 T209 K210 G86 I87 Y111 E154 D183 T185 S205 T207 K208
BS02 NLE A Y113 H115 K210 V338 S339 Y111 H113 K208 V336 S337 MOAD: Ki=0.6mM
BS03 PY6 A G88 I89 Y113 D185 S207 T209 K210 V338 S339 R374 G86 I87 Y111 D183 S205 T207 K208 V336 S337 R372
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:5m3z, PDBe:5m3z, PDBj:5m3z
PDBsum5m3z
PubMed28602917
UniProtA0A0A5P8W7

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