Structure for peptidase M01.005: alanyl aminopeptidase (bacterial-type)

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

PDB	Organism	Resolution	Comment
2DQ6_A	Escherichia coli	1.50 Å	mature
The catalytic zinc is shown as a light grey CPK sphere. The zinc ligands are shown in ball-and-stick representation: His296 and His300 in purple and Glu319 in blue. The catalytic residues are shown as Tyr297 in green and Glu280 in blue.

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TERTIARY STRUCTURE DATA
Comment	Resolution	PDB	PDBe	SCOP	CATH	PDBSum	Proteopedia	Reference
Escherichia coli
mature peptidase	1.50 Å	2DQ6	2DQ6	2DQ6	2DQ6	2DQ6	2DQ6	Ito et al., 2006
complex with bestatin	1.60 Å	2DQM	2DQM	2DQM	2DQM	2DQM	2DQM	Ito et al., 2006
structure of aminopeptidase n from e. coli suggests a compartmentalized, gated active site	1.65 Å	2HPO	2HPO	2HPO	2HPO	2HPO	2HPO	Addlagatta et al., 2006
complex with bestatin	2.30 Å	2HPT	2HPT	2HPT	2HPT	2HPT	2HPT	Addlagatta et al., 2006
mature peptidase	1.55 Å	2ZXG	2ZXG	2ZXG	2ZXG	2ZXG	2ZXG	Fournie-Zaluski et al., 2009
complex with arginine	2.00 Å	3B2P	3B2P	3B2P	3B2P	3B2P	3B2P	Addlagatta et al., 2008
complex with lysine	1.50 Å	3B2X	3B2X	3B2X	3B2X	3B2X	3B2X	Addlagatta et al., 2008
complex with phenylalanine	1.30 Å	3B34	3B34	3B34	3B34	3B34	3B34	Addlagatta et al., 2008
complex with tyrosine	1.70 Å	3B37	3B37	3B37	3B37	3B37	3B37	Addlagatta et al., 2008
complex with tryptophan	1.85 Å	3B3B	3B3B	3B3B	3B3B	3B3B	3B3B	Addlagatta et al., 2008
mature peptidase	2.30 Å	3KED	3KED	3KED	3KED	3KED	3KED	Gumpena et al., 2011
mature peptidase	2.15 Å	3PUU	3PUU	3PUU	3PUU	3PUU	3PUU	Gumpena et al., 2011
mature peptidase	1.45 Å	3QJX	3QJX	3QJX	3QJX	3QJX	3QJX	Gumpena et al., 2011
mature peptidase	1.90 Å	4Q4E	4Q4E	4Q4E	4Q4E	4Q4E	4Q4E	Ganji et al., 2015
mature peptidase	2.31 Å	4Q4I	4Q4I	4Q4I	4Q4I	4Q4I	4Q4I	Ganji et al., 2015
Met260Ala mutant; complex with l-2,3-diaminopropionic acid	2.00 Å	4XMT	4XMT	4XMT	4XMT	4XMT	4XMT
Met260Ala mutant; complex with L-alanine	2.91 Å	4XMU	4XMU	4XMU	4XMU	4XMU	4XMU
Met260Ala mutant; complex with l-arginine	2.92 Å	4XMV	4XMV	4XMV	4XMV	4XMV	4XMV
Met260Ala mutant; complex with l-aspartic acid	2.20 Å	4XMW	4XMW	4XMW	4XMW	4XMW	4XMW
Met260Ala mutant; complex with bestatin	2.30 Å	4XMX	4XMX	4XMX	4XMX	4XMX	4XMX
Met260Ala mutant; complex with 2,4-diaminobutyric acid	2.15 Å	4XMZ	4XMZ	4XMZ	4XMZ	4XMZ	4XMZ
Met260Ala mutant; complex with l-glutamate	2.20 Å	4XN1	4XN1	4XN1	4XN1	4XN1	4XN1
Met260Ala mutant; complex with l-leucine	2.11 Å	4XN2	4XN2	4XN2	4XN2	4XN2	4XN2
Met260Ala mutant; complex with l-methionine	1.99 Å	4XN4	4XN4	4XN4	4XN4	4XN4	4XN4
Met260Ala mutant; complex with l-phenylalanine	2.66 Å	4XN5	4XN5	4XN5	4XN5	4XN5	4XN5
complex with l-2,3- diaminopropionic acid	2.22 Å	4XN7	4XN7	4XN7	4XN7	4XN7	4XN7
complex with l- alanine	1.89 Å	4XN8	4XN8	4XN8	4XN8	4XN8	4XN8
complex with beta alanine	2.80 Å	4XN9	4XN9	4XN9	4XN9	4XN9	4XN9
complex with l-beta homolysine	2.40 Å	4XNA	4XNA	4XNA	4XNA	4XNA	4XNA
complex with l-beta homophenylalanine	1.95 Å	4XNB	4XNB	4XNB	4XNB	4XNB	4XNB
complex with l-beta homotryptophan	1.93 Å	4XND	4XND	4XND	4XND	4XND	4XND
complex with l- leucine	2.00 Å	4XO3	4XO3	4XO3	4XO3	4XO3	4XO3
complex with l- methionine	2.18 Å	4XO4	4XO4	4XO4	4XO4	4XO4	4XO4
complex with l- glutamate	1.98 Å	4XO5	4XO5	4XO5	4XO5	4XO5	4XO5
complex with 7- amino-5,7,8,9-tetrahydrobenzocyclohepten-6-one	1.40 Å	5MFR	5MFR	5MFR	5MFR	5MFR	5MFR
complex with 7- amino-4-phenyl-5,7,8,9-tetrahydrobenzocyclohepten-6-one	1.57 Å	5MFS	5MFS	5MFS	5MFS	5MFS	5MFS
complex with 7- amino-1-bromo-4-phenyl-5,7,8,9-tetrahydrobenzocyclohepten-6-one	1.59 Å	5MFT	5MFT	5MFT	5MFT	5MFT	5MFT
Glu298Ala mutant; complex with puromycin	2.50 Å	5YO1	5YO1	5YO1	5YO1	5YO1	5YO1
complex with o-methyl-l-tyrosine	1.58 Å	5YQ1	5YQ1	5YQ1	5YQ1	5YQ1	5YQ1
complex with puromycinaminonucleoside	1.60 Å	5YQ2	5YQ2	5YQ2	5YQ2	5YQ2	5YQ2
complex with puromycin	1.56 Å	5YQB	5YQB	5YQB	5YQB	5YQB	5YQB
e. coli aminopeptidase n solved by native sad from a dataset collectedin 60 second with jungfrau detector	2.37 Å	6G8B	6G8B	6G8B	6G8B	6G8B	6G8B