4XGP

Crystal Structure of E112A/H234A Mutant of Stationary Phase Survival Protein (SurE) from Salmonella typhimurium co-crystallized and soaked with AMP.

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
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
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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue MG A 301

Chain	Residue
A	ASP8
A	ASP9
A	SER39
A	ASN92
A	PO4302
A	HOH651
A	HOH656

---

site_id	AC2
Number of Residues	12
Details	binding site for residue PO4 A 302

Chain	Residue
A	GLY40
A	ASN92
A	ASN96
A	TYR103
A	SER104
A	GLY105
A	THR106
A	MG301
A	HOH656
A	HOH689
A	ASP8
A	SER39

---

site_id	AC3
Number of Residues	7
Details	binding site for residue ADE A 303

Chain	Residue
A	ASP100
A	ALA182
A	ILE199
A	GLY200
A	PRO201
A	PRO202
A	HOH690

---

site_id	AC4
Number of Residues	6
Details	binding site for residue MG B 301

Chain	Residue
B	ASP8
B	ASP9
B	ASN92
B	HOH619
B	HOH623
B	HOH624

---

site_id	AC5
Number of Residues	5
Details	binding site for residue EDO B 302

Chain	Residue
B	ALA182
B	GLY200
B	HOH665
B	HOH667
B	HOH680

---

site_id	AC6
Number of Residues	6
Details	binding site for residue MG C 301

Chain	Residue
C	ASP8
C	ASP9
C	ASN92
C	HOH563
C	HOH567
C	HOH568

---

site_id	AC7
Number of Residues	7
Details	binding site for residue EDO C 302

Chain	Residue
C	VAL11
C	HIS12
C	GLN17
C	PHE56
C	ASN58
C	ASP60
C	HOH475

---

site_id	AC8
Number of Residues	3
Details	binding site for residue EDO C 303

Chain	Residue
C	ILE199
C	GLY200
C	HOH610

---

site_id	AC9
Number of Residues	3
Details	binding site for residue EDO C 304

Chain	Residue
C	ASN96
C	TYR103
C	HOH573

---

site_id	AD1
Number of Residues	7
Details	binding site for residue MG D 301

Chain	Residue
D	ASP8
D	ASP9
D	ASN92
D	HOH525
D	HOH527
D	HOH576
D	HOH585

---

site_id	AD2
Number of Residues	5
Details	binding site for residue EDO D 302

Chain	Residue
D	GLY200
D	PRO201
D	PRO202
D	HOH579
D	HOH580

---

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

---