Structure of PDB 1cb7 Chain D

Receptor sequence
>1cb7D (length=483) Species: 1494 (Clostridium cochlearium) [Search protein sequence]
MELKNKKWTDEEFHKQREEVLQQWPTGKEVDLQEAVDYLKKIPAEKNFAE
KLVLAKKKGITMAQPRAGVALLDEHIELLRYLQDEGGADFLPSTIDAYTR
QNRYDECENGIKESEKAGRSLLNGFPGVNFGVKGCRKVLEAVNLPLQARH
GTPDSRLLAEIIHAGGWTSNEGGGISYNVPYAKNVTIEKSLLDWQYCDRL
VGFYEEQGVHINREPFGPLTGTLVPPSMSNAVGITEALLAAEQGVKNITV
GYGECGNMIQDIAALRCLEEQTNEYLKAYGYNDVFVTTVFHQWMGGFPQD
ESKAFGVIVTATTIAALAGATKVIVKTPHEAIGIPTKEANAAGIKATKMA
LNMLEGQRMPMSKELETEMAVIKAETKCILDKMFELGKGDLAIGTVKAFE
TGVMDIPFGPSKYNAGKMMPVRDNLGCVRYLEFGNVPFTEEIKNYNRERL
QERAKFEGRDVSFQMVIDDIFAVGKGRLIGRPE
3D structure
PDB1cb7 Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights.
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) R100 E171
Catalytic site (residue number reindexed from 1) R100 E171
Enzyme Commision number 5.4.99.1: methylaspartate mutase.
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 COB D R100 Y181 T220 M294 G295 G296 F297 E330 G333 I334 F471 R100 Y181 T220 M294 G295 G296 F297 E330 G333 I334 F471
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0016853 isomerase activity
GO:0016866 intramolecular transferase activity
GO:0031419 cobalamin binding
GO:0050097 methylaspartate mutase activity
Biological Process
GO:0019553 glutamate catabolic process via L-citramalate
GO:0019670 anaerobic glutamate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1cb7, PDBe:1cb7, PDBj:1cb7
PDBsum1cb7
PubMed10467146
UniProtP80077|GLME_CLOCO Glutamate mutase epsilon subunit (Gene Name=glmE)

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