6YRA

Crystal structure of ATP-dependent caprolactamase from Pseudomonas jessenii

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0006749	biological_process	glutathione metabolic process
A	0016787	molecular_function	hydrolase activity
A	0017168	molecular_function	5-oxoprolinase (ATP-hydrolyzing) activity
B	0003824	molecular_function	catalytic activity
B	0005829	cellular_component	cytosol
B	0006749	biological_process	glutathione metabolic process
B	0016787	molecular_function	hydrolase activity
B	0017168	molecular_function	5-oxoprolinase (ATP-hydrolyzing) activity
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0006749	biological_process	glutathione metabolic process
C	0016787	molecular_function	hydrolase activity
C	0017168	molecular_function	5-oxoprolinase (ATP-hydrolyzing) activity
D	0003824	molecular_function	catalytic activity
D	0005829	cellular_component	cytosol
D	0006749	biological_process	glutathione metabolic process
D	0016787	molecular_function	hydrolase activity
D	0017168	molecular_function	5-oxoprolinase (ATP-hydrolyzing) activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN B 600

Chain	Residue
B	ASP41
B	HIS99
B	ASP102
B	HIS124

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site_id	AC2
Number of Residues	4
Details	binding site for residue ZN D 600

Chain	Residue
D	ASP41
D	HIS99
D	ASP102
D	HIS124

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33826169","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6YRA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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