Structure of PDB 3i12 Chain D

Receptor sequence
>3i12D (length=355) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium) [Search protein sequence]
KLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKTRFDVVLLGIDKAGQWHVN
DAENYLQNADDPAHIALRPSAISLAQVPGKHQHQLINAQNGQPLPTVDVI
FPIVHGTLGEDGSLQGMLRVANLPFVGSDVLSSAACMDKDVAKRLLRDAG
LNIAPFITLTRTNRHAFSFAEVESRLGLPLFVKPANQGSSVGVSKVANEA
QYQQAVALAFEFDHKVVVEQGIKGREIECAVLGNDNPQASTCGEIVLNSE
FYIDDNGAQVVVPAQIPSEVNDKIRAIAIQAYQTLGCAGMARVDVFLTAD
NEVVINEINTLPGFTNISMYPKLWQASGLGYTDLISRLIELALERHTANN
ALKTT
3D structure
PDB3i12 The crystal structure of the D-alanyl-alanine synthetase A from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
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) E16 V19 Q22 H107 S191 Y260 D263 R300 D302 E315 N317 G321 I325
Catalytic site (residue number reindexed from 1) E14 V17 Q20 H105 S189 Y252 D255 R292 D294 E307 N309 G313 I317
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 K141 F183 K185 S191 S192 E221 Q222 G223 I224 E228 F304 E315 K139 F181 K183 S189 S190 E219 Q220 G221 I222 E226 F296 E307
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:3i12, PDBe:3i12, PDBj:3i12
PDBsum3i12
PubMed
UniProtP0A1F0|DDLA_SALTY D-alanine--D-alanine ligase A (Gene Name=ddlA)

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