Structure of PDB 2zdg Chain D

Receptor sequence
>2zdgD (length=304) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MRVLLIAGGVSPEHEVSLLSAEGVLRHIPFPTDLAVIAQDGRWLLGEKAL
TALEAKAAPEGEHPFPPPLSWERYDVVFPLLHGRFGEDGTVQGFLELLGK
PYVGAGVAASALCMDKDLSKRVLAQAGVPVVPWVAVRKGEPPVVPFDPPF
FVKPANTGSSVGISRVERFQDLEAALALAFRYDEKAVVEKALSPVRELEV
GVLGNVFGEASPVGEVRYEAPAELLIPAPLTQETVQELALKAYKVLGVRG
MARVDFFLAEGELYLNELNTIPGFTPTSMYPRLFEAGGVAYPELLRRLVE
LALT
3D structure
PDB2zdg Crystal structure of D-Alanine:D-Alanine Ligase with ADP from Thermus thermophius HB8
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E13 V16 L19 H82 S159 R268 D270 E282 N284 G288 T292
Catalytic site (residue number reindexed from 1) E13 V16 L19 H82 S159 R253 D255 E267 N269 G273 T277
Enzyme Commision number 6.3.2.4: D-alanine--D-alanine ligase.
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 ADP D K116 F151 K153 S160 L192 E197 F272 E282 K116 F151 K153 S160 L192 E197 F257 E267
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0008716 D-alanine-D-alanine ligase activity
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2zdg, PDBe:2zdg, PDBj:2zdg
PDBsum2zdg
PubMed
UniProtQ5SHZ3|DDL_THET8 D-alanine--D-alanine ligase (Gene Name=ddl)

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