Structure of PDB 1ec7 Chain B

Receptor sequence

>1ec7B (length=440) Species: 562 (Escherichia coli)

FTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGE
IPGGEKIRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDGRGLQTFDL
RTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGN
RKATPLPYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFNDFKL
KGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNEAIKIGKYLKGSL
AYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQS
VDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAA
AAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDMDQ
VMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR

3D structure

• PDB: 1ec7 Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli.
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K205 K207 D235 N237 E260 N289 M290 D313 H339 N341 I365
• Catalytic site (residue number reindexed from 1): K199 K201 D229 N231 E254 N283 M284 D307 H333 N335 I359
• Enzyme Commision number: 4.2.1.40: glucarate dehydratase.

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	MG	B	D235 E260 N289	D229 E254 N283

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0008872 glucarate dehydratase activity
• GO:0016829 lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0019394 glucarate catabolic process
• GO:0042838 D-glucarate catabolic process

External links

• PDB: RCSB:1ec7, PDBe:1ec7, PDBj:1ec7
• PDBsum: 1ec7
• PubMed: 10769114
• UniProt: P0AES2|GUDD_ECOLI Glucarate dehydratase (Gene Name=gudD)