Structure of PDB 1pmo Chain E

Receptor sequence
>1pmoE (length=463) Species: 562 (Escherichia coli) [Search protein sequence]
KQVTDLRSELLDSRFGAKSISTIAESKRFPLHEMRDDVAFQIINDELYLD
GNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNM
VADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTD
KPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTI
GVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPF
VAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNV
DYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYL
ADEIAKLGPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRG
WQVPAFTLGGEATDIVVMRIMCRRGFEMDFAELLLEDYKASLKYLSDHPK
LQGIAQQNSFKHT
3D structure
PDB1pmo Crystal structure and functional analysis of escherichia coli glutamate decarboxylase
ChainE
Resolution2.3 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 PLR E S126 S127 Q163 T212 D243 A245 H275 K276 T466 S123 S124 Q160 T209 D240 A242 H272 K273 T463
BS02 PLR E F317 S318 F314 S315
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1pmo, PDBe:1pmo, PDBj:1pmo
PDBsum1pmo
PubMed12912902
UniProtP69910|DCEB_ECOLI Glutamate decarboxylase beta (Gene Name=gadB)

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