Structure of PDB 1ccw Chain B

Receptor sequence

>1ccwB (length=483) Species: 1494 (Clostridium cochlearium)

MELKNKKWTDEEFHKQREEVLQQWPTGKEVDLQEAVDYLKKIPAEKNFAE
KLVLAKKKGITMAQPRAGVALLDEHIELLRYLQDEGGADFLPSTIDAYTR
QNRYDECENGIKESEKAGRSLLNGFPGVNFGVKGCRKVLEAVNLPLQARH
GTPDSRLLAEIIHAGGWTSNEGGGISYNVPYAKNVTIEKSLLDWQYCDRL
VGFYEEQGVHINREPFGPLTGTLVPPSMSNAVGITEALLAAEQGVKNITV
GYGECGNMIQDIAALRCLEEQTNEYLKAYGYNDVFVTTVFHQWMGGFPQD
ESKAFGVIVTATTIAALAGATKVIVKTPHEAIGIPTKEANAAGIKATKMA
LNMLEGQRMPMSKELETEMAVIKAETKCILDKMFELGKGDLAIGTVKAFE
TGVMDIPFGPSKYNAGKMMPVRDNLGCVRYLEFGNVPFTEEIKNYNRERL
QERAKFEGRDVSFQMVIDDIFAVGKGRLIGRPE

3D structure

• PDB: 1ccw Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights
• Chain: B
• Resolution: 1.6 Å

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	CNC	B	R100 Y181 T220 M294 G295 G296 F297 E330 A331 G333 I334 F471	R100 Y181 T220 M294 G295 G296 F297 E330 A331 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

External links

• PDB: RCSB:1ccw, PDBe:1ccw, PDBj:1ccw
• PDBsum: 1ccw
• PubMed: 10467146
• UniProt: P80077|GLME_CLOCO Glutamate mutase epsilon subunit (Gene Name=glmE)