Structure of PDB 2y2b Chain A

Receptor sequence
>2y2bA (length=179) Species: 546 (Citrobacter freundii) [Search protein sequence]
MLLDEGWLAEARRVPSPHYDCRPDDENPSLLVVHNISLPPGEFGGPWIDA
LFTGTIDPNAHPYFAGIAHLRVSAHCLIRRDGEIVQYVPFDKRAWHAGVS
SYQGRERCNDFSIGIELEGTDTLAYTDAQYQQLAAVTNALITRYPAIANN
MTGHCNIAPERKTDPGPSFDWARFRALVT
3D structure
PDB2y2b Crystal Structures of Bacterial Peptidoglycan Amidase Ampd and an Unprecedented Activation Mechanism.
ChainA
Resolution1.9 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 3.5.1.28: N-acetylmuramoyl-L-alanine amidase.
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 AH0 A N35 I36 L38 L51 Y63 K162 D164 N35 I36 L38 L51 Y63 K162 D164
BS02 MHI A H34 F52 R71 V72 W95 H96 A97 G98 R107 N109 E116 H154 R161 H34 F52 R71 V72 W95 H96 A97 G98 R107 N109 E116 H154 R161
BS03 ZN A H34 H154 D164 H34 H154 D164
Gene Ontology
Molecular Function
GO:0008745 N-acetylmuramoyl-L-alanine amidase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0009253 peptidoglycan catabolic process
GO:0009254 peptidoglycan turnover
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2y2b, PDBe:2y2b, PDBj:2y2b
PDBsum2y2b
PubMed21775432
UniProtP82974|AMPD_CITFR 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD (Gene Name=ampD)

[Back to BioLiP]