Structure of PDB 1ko0 Chain A

Receptor sequence
>1ko0A (length=419) Species: 562 (Escherichia coli) [Search protein sequence]
PHSLFSTDTDLTAENLLRLPAEFGCPVWVYDAQIIRRQIAALKQFDVVRF
AQKACSNIHILRLMREQGVKVDSVSLGEIERALAAGYNPQTHPDDIVFTA
DVIDQATLERVSELQIPVNAGSVDMLDQLGQVSPGHRVWLRVNPGFGHGH
SQKTNTGGENSKHGIWYTDLPAALDVIQRHHLQLVGIHMHIGSGVDYAHL
EQVCGAMVRQVIEFGQDLQAISAGGGLSVPYQQGEEAVDTEHYYGLWNAA
REQIARHLGHPVKLEIEPGRFLVAQSGVLITQVRSVKQMGSRHFVLVDAG
FNDLMRPAMYGSYHHISALAADGRSLEHAPTVETVVAGPLCESGDVFTQQ
EGGNVETRALPEVKAGDYLVLHDTGAYGASMSSNYNSRPLLPEVLFDNGQ
ARLIRRRQTIEELLALELL
3D structure
PDB1ko0 Diaminopimelate Decarboxylase uses a Versatile Active Site for Stereospecific Decarboxylation
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.20: diaminopimelate 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 A A52 K54 H191 G227 E268 P269 G270 R271 Y378 A51 K53 H190 G226 E267 P268 G269 R270 Y377
BS02 LYS A K54 R271 R307 Y311 Y378 K53 R270 R306 Y310 Y377
BS03 DLY A K54 T157 H191 Y311 Y378 K53 T156 H190 Y310 Y377
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0008836 diaminopimelate decarboxylase activity
GO:0016830 carbon-carbon lyase activity
GO:0016831 carboxy-lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0009085 lysine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate

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Molecular Function
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Biological Process
External links
PDB RCSB:1ko0, PDBe:1ko0, PDBj:1ko0
PDBsum1ko0
PubMed
UniProtP00861|DCDA_ECOLI Diaminopimelate decarboxylase (Gene Name=lysA)

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