Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5YOX

HD domain-containing protein YGK1(YGL101W)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002953	molecular_function	5'-deoxynucleotidase activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0008270	molecular_function	zinc ion binding
A	0009159	biological_process	deoxyribonucleoside monophosphate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0050484	molecular_function	GMP 5'-nucleotidase activity
B	0002953	molecular_function	5'-deoxynucleotidase activity
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0008270	molecular_function	zinc ion binding
B	0009159	biological_process	deoxyribonucleoside monophosphate catabolic process
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0050484	molecular_function	GMP 5'-nucleotidase activity
C	0002953	molecular_function	5'-deoxynucleotidase activity
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0008270	molecular_function	zinc ion binding
C	0009159	biological_process	deoxyribonucleoside monophosphate catabolic process
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
C	0050484	molecular_function	GMP 5'-nucleotidase activity
D	0002953	molecular_function	5'-deoxynucleotidase activity
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0008270	molecular_function	zinc ion binding
D	0009159	biological_process	deoxyribonucleoside monophosphate catabolic process
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding
D	0050484	molecular_function	GMP 5'-nucleotidase activity
E	0002953	molecular_function	5'-deoxynucleotidase activity
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0008270	molecular_function	zinc ion binding
E	0009159	biological_process	deoxyribonucleoside monophosphate catabolic process
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding
E	0050484	molecular_function	GMP 5'-nucleotidase activity
F	0002953	molecular_function	5'-deoxynucleotidase activity
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0008270	molecular_function	zinc ion binding
F	0009159	biological_process	deoxyribonucleoside monophosphate catabolic process
F	0016787	molecular_function	hydrolase activity
F	0046872	molecular_function	metal ion binding
F	0050484	molecular_function	GMP 5'-nucleotidase activity
G	0002953	molecular_function	5'-deoxynucleotidase activity
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0008270	molecular_function	zinc ion binding
G	0009159	biological_process	deoxyribonucleoside monophosphate catabolic process
G	0016787	molecular_function	hydrolase activity
G	0046872	molecular_function	metal ion binding
G	0050484	molecular_function	GMP 5'-nucleotidase activity
H	0002953	molecular_function	5'-deoxynucleotidase activity
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0008270	molecular_function	zinc ion binding
H	0009159	biological_process	deoxyribonucleoside monophosphate catabolic process
H	0016787	molecular_function	hydrolase activity
H	0046872	molecular_function	metal ion binding
H	0050484	molecular_function	GMP 5'-nucleotidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 300

Chain	Residue
A	HIS61
A	HIS89
A	ASP90
A	ASP159

site_id	AC2
Number of Residues	5
Details	binding site for residue ZN B 300

Chain	Residue
B	ARG43
B	HIS61
B	HIS89
B	ASP90
B	ASP159

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN C 300

Chain	Residue
C	HIS61
C	HIS89
C	ASP90
C	ASP159

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN D 300

Chain	Residue
D	HIS61
D	HIS89
D	ASP90
D	ASP159

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN E 300

Chain	Residue
E	HIS61
E	HIS89
E	ASP90
E	ASP159

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN F 300

Chain	Residue
F	HIS61
F	HIS89
F	ASP90
F	ASP159

site_id	AC7
Number of Residues	3
Details	binding site for residue ZN G 300

Chain	Residue
G	HIS61
G	ASP90
G	ASP159

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN H 300

Chain	Residue
H	HIS61
H	HIS89
H	ASP90
H	ASP159

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269\|PubMed:29752939, ECO:0007744\|PDB:5YOX

Chain	Residue	Details
A	HIS61
C	HIS89
C	ASP90
C	ASP159
D	HIS61
D	HIS89
D	ASP90
D	ASP159
E	HIS61
E	HIS89
E	ASP90
A	HIS89
E	ASP159
F	HIS61
F	HIS89
F	ASP90
F	ASP159
G	HIS61
G	HIS89
G	ASP90
G	ASP159
H	HIS61
A	ASP90
H	HIS89
H	ASP90
H	ASP159
A	ASP159
B	HIS61
B	HIS89
B	ASP90
B	ASP159
C	HIS61

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q7Z4H3

Chain	Residue	Details
A	GLU93
D	GLU93
D	ASP98
D	ILE99
E	GLU93
E	ASP98
E	ILE99
F	GLU93
F	ASP98
F	ILE99
G	GLU93
A	ASP98
G	ASP98
G	ILE99
H	GLU93
H	ASP98
H	ILE99
A	ILE99
B	GLU93
B	ASP98
B	ILE99
C	GLU93
C	ASP98
C	ILE99

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)