Structure for peptidase M24.004: aminopeptidase P (bacteria)

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates

PDB	Organism	Resolution	Comment
1A16	Escherichia coli	2.30 Å	complex with inhibitor Pro-Leu
The catalytic manganese ions are shown as grey CPK spheres. The manganese ligands are shown in ball-and-stick representation: Asp260 and Asp271 in light pink, His354 in purple, and Glu383 and Glu406 in dark blue. The inhibitor Pro-Leu is shown in ball-and-stick representation in grey.

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TERTIARY STRUCTURE DATA
Comment	Resolution	PDB	PDBe	SCOP	CATH	PDBSum	Proteopedia	Reference
Escherichia coli
complex with inhibitor Pro-Leu	2.30 Å	1A16	1A16	1A16	1A16	1A16	1A16	Wilce et al., 1998
mature peptidase	2.00 Å	1AZ9	1AZ9	1AZ9	1AZ9	1AZ9	1AZ9	Graham et al., 2005
low pH form	2.70 Å	1JAW	1JAW	1JAW	1JAW	1JAW	1JAW	Wilce et al., 1998
mature peptidase	2.40 Å	1M35	1M35	1M35	1M35	1M35	1M35	Graham et al., 2003
complex with the inhibitor apstatin	2.30 Å	1N51	1N51	1N51	1N51	1N51	1N51	Graham et al., 2004
ca-substituted form of e. coli aminopeptidase p	2.40 Å	1W2M	1W2M	1W2M	1W2M	1W2M	1W2M	Graham et al., 2005
znmg substituted aminopeptidase p from e. coli	2.00 Å	1W7V	1W7V	1W7V	1W7V	1W7V	1W7V	Graham et al., 2005
zn mg substituted aminopeptidase p from e. coli	2.30 Å	1WBQ	1WBQ	1WBQ	1WBQ	1WBQ	1WBQ	Graham et al., 2005
mg-substituted form of e. coli aminopeptidase p	2.00 Å	1WL6	1WL6	1WL6	1WL6	1WL6	1WL6	Graham et al., 2005
structure of aminopeptidase p from e. coli	1.90 Å	1WL9	1WL9	1WL9	1WL9	1WL9	1WL9	Graham et al., 2005
apo aminopeptidase p from e. coli	2.10 Å	1WLR	1WLR	1WLR	1WLR	1WLR	1WLR	Graham et al., 2005
Zn substituted; complex with product	2.40 Å	2BH3	2BH3	2BH3	2BH3	2BH3	2BH3	Graham et al., 2005
complex with substrate	2.40 Å	2BHA	2BHA	2BHA	2BHA	2BHA	2BHA	Graham et al., 2005
zn substituted e. coli aminopeptidase p	2.41 Å	2BHB	2BHB	2BHB	2BHB	2BHB	2BHB	Graham et al., 2005
na substituted e. coli aminopeptidase p	2.40 Å	2BHC	2BHC	2BHC	2BHC	2BHC	2BHC	Graham et al., 2005
Mg substituted; complex with product	2.50 Å	2BHD	2BHD	2BHD	2BHD	2BHD	2BHD	Graham et al., 2005
mn substituted e. coli aminopeptidase p in complex with product and zn	2.40 Å	2BN7	2BN7	2BN7	2BN7	2BN7	2BN7	Graham et al., 2005
his243ala escherichia coli aminopeptidase p	1.75 Å	2BWS	2BWS	2BWS	2BWS	2BWS	2BWS	Graham et al., 2006
asp260ala escherichia coli aminopeptidase p	2.90 Å	2BWT	2BWT	2BWT	2BWT	2BWT	2BWT	Graham et al., 2006
asp271ala escherichia coli aminopeptidase p	2.20 Å	2BWU	2BWU	2BWU	2BWU	2BWU	2BWU	Graham et al., 2006
his361ala escherichia coli aminopeptidase p	1.70 Å	2BWV	2BWV	2BWV	2BWV	2BWV	2BWV	Graham et al., 2006
his350ala escherichia coli aminopeptidase p	2.61 Å	2BWW	2BWW	2BWW	2BWW	2BWW	2BWW	Graham et al., 2006
his354ala escherichia coli aminopeptidase p	1.70 Å	2BWX	2BWX	2BWX	2BWX	2BWX	2BWX	Graham et al., 2006
glu383ala escherichia coli aminopeptidase p	2.40 Å	2BWY	2BWY	2BWY	2BWY	2BWY	2BWY	Graham et al., 2006
His243Ala mutant; complex with substrate	1.70 Å	2V3X	2V3X	2V3X	2V3X	2V3X	2V3X	Graham & Guss, 2008
His361Ala mutant; complex with product	1.60 Å	2V3Y	2V3Y	2V3Y	2V3Y	2V3Y	2V3Y	Graham & Guss, 2008
Glu383Ala mutant; complex with substrate	1.56 Å	2V3Z	2V3Z	2V3Z	2V3Z	2V3Z	2V3Z	Graham & Guss, 2008
Pseudomonas aeruginosa
the structure of pseudomonas aeruginosa aminopeptidase pepp	1.78 Å	5WZE	5WZE	5WZE	5WZE	5WZE	5WZE
Yersinia pestis
proline aminopeptidase p ii from yersinia pestis	1.76 Å	4PV4	4PV4	4PV4	4PV4	4PV4	4PV4