Structure of PDB 1cb7 Chain C

Receptor sequence
>1cb7C (length=137) Species: 1494 (Clostridium cochlearium) [Search protein sequence]
MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAA
IETKADAILVSSLYGQGEIDCKGLRQKCDEAGLEGILLYVGGNIVVGKQH
WPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE
3D structure
PDB1cb7 Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights.
ChainC
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) V10 D14 H16
Catalytic site (residue number reindexed from 1) V10 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 COB C D14 C15 H16 A17 G19 S61 L63 Y64 G65 G91 G92 N93 V95 V96 T121 P123 D14 C15 H16 A17 G19 S61 L63 Y64 G65 G91 G92 N93 V95 V96 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1cb7, PDBe:1cb7, PDBj:1cb7
PDBsum1cb7
PubMed10467146
UniProtP80078|GMSS_CLOCO Glutamate mutase sigma subunit (Gene Name=glmS)

[Back to BioLiP]