7QUN

CryoEM structure of mammalian AAP in complex with Meropenem

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0008242	molecular_function	omega peptidase activity
A	0016787	molecular_function	hydrolase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008236	molecular_function	serine-type peptidase activity
B	0008242	molecular_function	omega peptidase activity
B	0016787	molecular_function	hydrolase activity
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005737	cellular_component	cytoplasm
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0008236	molecular_function	serine-type peptidase activity
C	0008242	molecular_function	omega peptidase activity
C	0016787	molecular_function	hydrolase activity
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005737	cellular_component	cytoplasm
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0008236	molecular_function	serine-type peptidase activity
D	0008242	molecular_function	omega peptidase activity
D	0016787	molecular_function	hydrolase activity

Functional Information from PROSITE/UniProt

site_id	PS00708
Number of Residues	31
Details	PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DvqfAveqVlqeehfdagrvalmGgShGGFL

Chain	Residue	Details
A	ASP562-LEU592

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:8576092

Chain	Residue	Details
A	SER587
B	SER587
C	SER587
D	SER587

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site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084

Chain	Residue	Details
A	ASP675
A	HIS707
B	ASP675
B	HIS707
C	ASP675
C	HIS707
D	ASP675
D	HIS707

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site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2691504, ECO:0000269|PubMed:8576092

Chain	Residue	Details
A	MET1
B	MET1
C	MET1
D	MET1

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13798

Chain	Residue	Details
A	SER187
B	SER187
C	SER187
D	SER187

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