9GOU

Cryo-EM structure of acylaminoacyl-peptidase in complex with dichlorvos

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005737	cellular_component	cytoplasm
A	0008233	molecular_function	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	0008233	molecular_function	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	0008233	molecular_function	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	0008233	molecular_function	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	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8576092","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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