Structure of PDB 2dgk Chain D

Receptor sequence
>2dgkD (length=438) Species: 562 (Escherichia coli) [Search protein sequence]
SKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDL
SINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSE
ACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELR
EIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALD
KFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFG
LAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRPAGQVIAQY
YEFLRLGREGYTKVQNASYQVAAYLADEIAKLGPYEFICTGRPDEGIPAV
CFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVVMRIMCRRG
FEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT
3D structure
PDB2dgk Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB
ChainD
Resolution1.9 Å
3D
structure
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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 D F317 S318 F289 S290
BS02 PLP D G125 S126 S127 Q163 T212 D243 A245 S273 H275 K276 H465 G97 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

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Biological Process
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Cellular Component
External links
PDB RCSB:2dgk, PDBe:2dgk, PDBj:2dgk
PDBsum2dgk
PubMed16675957
UniProtP69910|DCEB_ECOLI Glutamate decarboxylase beta (Gene Name=gadB)

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