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Structure of PDB 1pmm Chain C

Receptor sequence >1pmmC (length=449) Species: 562 (Escherichia coli) [Search protein sequence] KQVTDLRSELLDSRFGAKSISTIAESKRFPLHEMRDDVAFQIINDELYLD GNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNM VADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTD KPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTI GVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPF VAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNV DYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYL ADEIAKLGPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRG WQVPAFTLGGEATDIVVMRIMCRRGFEMDFAELLLEDYKASLKYLSDHP

3D structure PDB 1pmm Crystal structure and functional analysis of escherichia coli glutamate decarboxylase Chain C Resolution 2.0 Å 3D structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

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 C S126 S127 Q163 T212 D243 A245 H275 K276 S123 S124 Q160 T209 D240 A242 H272 K273 BS02 PLP C 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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