Structure of PDB 6h9e Chain C

Receptor sequence
>6h9eC (length=137) Species: 1494 (Clostridium cochlearium) [Search protein sequence]
MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQENFIKAA
IETKADAILVSSLYGQGEIDCKGLRQKCDEAGLEGILLYVGGNIVVGKQH
WPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE
3D structure
PDB6h9e Structure-Based Demystification of Radical Catalysis by a Coenzyme B 12 Dependent Enzyme-Crystallographic Study of Glutamate Mutase with Cofactor Homologues.
ChainC
Resolution1.82 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D14 H16
Catalytic site (residue number reindexed from 1) D14 H16
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 B12 C S13 C15 H16 A17 V18 G19 I22 L23 S61 L63 Y64 G65 G91 G92 N93 V95 V96 Y117 T121 P123 S13 C15 H16 A17 V18 G19 I22 L23 S61 L63 Y64 G65 G91 G92 N93 V95 V96 Y117 T121 P123
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016853 isomerase activity
GO:0016866 intramolecular transferase activity
GO:0031419 cobalamin binding
GO:0046872 metal ion 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:6h9e, PDBe:6h9e, PDBj:6h9e
PDBsum6h9e
PubMed35793207
UniProtP80078|GMSS_CLOCO Glutamate mutase sigma subunit (Gene Name=glmS)

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