3MKN

Crystal structure of the E. coli pyrimidine nucleosidase YeiK bound to a competitive inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006206	biological_process	pyrimidine nucleobase metabolic process
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
A	0045437	molecular_function	uridine nucleosidase activity
A	0046133	biological_process	pyrimidine ribonucleoside catabolic process
A	0046872	molecular_function	metal ion binding
A	0050263	molecular_function	ribosylpyrimidine nucleosidase activity
B	0005509	molecular_function	calcium ion binding
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006206	biological_process	pyrimidine nucleobase metabolic process
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
B	0045437	molecular_function	uridine nucleosidase activity
B	0046133	biological_process	pyrimidine ribonucleoside catabolic process
B	0046872	molecular_function	metal ion binding
B	0050263	molecular_function	ribosylpyrimidine nucleosidase activity
C	0005509	molecular_function	calcium ion binding
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006206	biological_process	pyrimidine nucleobase metabolic process
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
C	0045437	molecular_function	uridine nucleosidase activity
C	0046133	biological_process	pyrimidine ribonucleoside catabolic process
C	0046872	molecular_function	metal ion binding
C	0050263	molecular_function	ribosylpyrimidine nucleosidase activity
D	0005509	molecular_function	calcium ion binding
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006206	biological_process	pyrimidine nucleobase metabolic process
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
D	0045437	molecular_function	uridine nucleosidase activity
D	0046133	biological_process	pyrimidine ribonucleoside catabolic process
D	0046872	molecular_function	metal ion binding
D	0050263	molecular_function	ribosylpyrimidine nucleosidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 501

Chain	Residue
A	ASP11
A	ASP16
A	ASN40
A	VAL124
A	ASP240
A	HOH314
A	DNB502

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site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DNB A 502

Chain	Residue
A	ASN40
A	ILE81
A	HIS82
A	VAL124
A	MET150
A	ASN158
A	GLU164
A	PHE165
A	ASN166
A	ASP240
A	HOH314
A	CA501
A	ASP15
A	ASP16

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA B 501

Chain	Residue
B	ASP11
B	ASP16
B	ASN40
B	VAL124
B	ASP240
B	HOH315
B	DNB502

---

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DNB B 502

Chain	Residue
B	ASP15
B	ASP16
B	ASN40
B	VAL124
B	MET150
B	ASN158
B	GLU164
B	ASN166
B	HIS239
B	ASP240
B	HOH315
B	HOH330
B	CA501

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA C 501

Chain	Residue
C	ASP11
C	ASP16
C	ASN40
C	VAL124
C	ASP240
C	HOH314
C	DNB502

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DNB C 502

Chain	Residue
C	ASP15
C	ASP16
C	ASN40
C	ALA78
C	VAL124
C	MET150
C	ASN158
C	GLU164
C	ASN166
C	ASP240
C	HOH314
C	CA501

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 501

Chain	Residue
D	ASP11
D	ASP16
D	VAL124
D	ASP240
D	HOH314
D	DNB502

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DNB D 502

Chain	Residue
D	ASP15
D	ASP16
D	ASN40
D	ASN80
D	ILE81
D	HIS82
D	VAL124
D	MET150
D	ASN158
D	GLU164
D	PHE165
D	ASN166
D	ASP240
D	HOH314
D	CA501
D	HOH542

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Functional Information from PROSITE/UniProt

site_id	PS01247
Number of Residues	11
Details	IUNH Inosine-uridine preferring nucleoside hydrolase family signature. DcDPGhDDAIA

Chain	Residue	Details
A	ASP9-ALA19

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