4XER

Crystal Structure of C2 form of E112A/H234A Mutant of Stationary Phase Survival Protein (SurE) from Salmonella typhimurium

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004309	molecular_function	exopolyphosphatase activity
A	0005737	cellular_component	cytoplasm
A	0008252	molecular_function	nucleotidase activity
A	0008253	molecular_function	5'-nucleotidase activity
A	0008254	molecular_function	3'-nucleotidase activity
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0106411	molecular_function	XMP 5'-nucleosidase activity
B	0000166	molecular_function	nucleotide binding
B	0004309	molecular_function	exopolyphosphatase activity
B	0005737	cellular_component	cytoplasm
B	0008252	molecular_function	nucleotidase activity
B	0008253	molecular_function	5'-nucleotidase activity
B	0008254	molecular_function	3'-nucleotidase activity
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0106411	molecular_function	XMP 5'-nucleosidase activity
C	0000166	molecular_function	nucleotide binding
C	0004309	molecular_function	exopolyphosphatase activity
C	0005737	cellular_component	cytoplasm
C	0008252	molecular_function	nucleotidase activity
C	0008253	molecular_function	5'-nucleotidase activity
C	0008254	molecular_function	3'-nucleotidase activity
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
C	0106411	molecular_function	XMP 5'-nucleosidase activity
D	0000166	molecular_function	nucleotide binding
D	0004309	molecular_function	exopolyphosphatase activity
D	0005737	cellular_component	cytoplasm
D	0008252	molecular_function	nucleotidase activity
D	0008253	molecular_function	5'-nucleotidase activity
D	0008254	molecular_function	3'-nucleotidase activity
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding
D	0106411	molecular_function	XMP 5'-nucleosidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue ACT A 301

Chain	Residue
A	ALA182
A	GLY200
A	HOH685

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site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 302

Chain	Residue
A	ASP8
A	ASP9
A	SER39
A	ASN92
A	HOH482
A	HOH483

---

site_id	AC3
Number of Residues	6
Details	binding site for residue PO4 B 301

Chain	Residue
B	PRO95
B	ASN96
B	ASP100
B	HOH457
B	HOH533
B	HOH617

---

site_id	AC4
Number of Residues	5
Details	binding site for residue MPD B 302

Chain	Residue
B	ALA182
B	GLY200
B	PRO202
B	HOH554
B	HOH640

---

site_id	AC5
Number of Residues	6
Details	binding site for residue MG B 303

Chain	Residue
B	ASP8
B	ASP9
B	ASN92
B	HOH451
B	HOH456
B	HOH457

---

site_id	AC6
Number of Residues	3
Details	binding site for residue PO4 C 301

Chain	Residue
C	ASN96
C	ASP100
C	HOH581

---

site_id	AC7
Number of Residues	6
Details	binding site for residue MG C 302

Chain	Residue
C	ASP8
C	ASP9
C	ASN92
C	HOH419
C	HOH423
C	HOH555

---

site_id	AC8
Number of Residues	5
Details	binding site for residue MG D 301

Chain	Residue
D	ASP8
D	ASP9
D	SER39
D	ASN92
D	HOH523

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00060

Chain	Residue	Details
A	ASP8
C	ASP9
C	SER39
C	ASN92
D	ASP8
D	ASP9
D	SER39
D	ASN92
A	ASP9
A	SER39
A	ASN92
B	ASP8
B	ASP9
B	SER39
B	ASN92
C	ASP8

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