Structure of PDB 2dgk Chain B

Receptor sequence

>2dgkB (length=438) Species: 562 (Escherichia coli)

SKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDL
SINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSE
ACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELR
EIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALD
KFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFG
LAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRPAGQVIAQY
YEFLRLGREGYTKVQNASYQVAAYLADEIAKLGPYEFICTGRPDEGIPAV
CFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVVMRIMCRRG
FEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT

3D structure

• PDB: 2dgk Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Enzyme Commision number: 4.1.1.15: glutamate decarboxylase.

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	PLP	B	F317 S318	F289 S290
BS02	PLP	B	S126 S127 Q163 T212 D243 A245 S273 H275 K276 H465	S98 S99 Q135 T184 D215 A217 S245 H247 K248 H437

Gene Ontology

Molecular Function

• GO:0004351 glutamate decarboxylase activity
• GO:0005515 protein binding
• GO:0016830 carbon-carbon lyase activity
• GO:0016831 carboxy-lyase activity
• GO:0030170 pyridoxal phosphate binding

Biological Process

• GO:0006536 glutamate metabolic process
• GO:0006538 glutamate catabolic process
• GO:0019752 carboxylic acid metabolic process
• GO:0051454 intracellular pH elevation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0016020 membrane

External links

• PDB: RCSB:2dgk, PDBe:2dgk, PDBj:2dgk
• PDBsum: 2dgk
• PubMed: 16675957
• UniProt: P69910|DCEB_ECOLI Glutamate decarboxylase beta (Gene Name=gadB)