Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RYU

Crystal Structure of C2 form of E112A 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	6
Details	BINDING SITE FOR RESIDUE PO4 A 301

Chain	Residue
A	ASN96
A	ASP100
A	HOH413
A	HOH414
A	HOH434
A	HOH580

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 302

Chain	Residue
A	PRO201
A	PRO202
A	HOH615
A	HOH638
B	LEU45
B	TYR73
A	ALA182
A	ILE199
A	GLY200

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 303

Chain	Residue
A	TYR73
A	ALA112
A	HOH582
A	HOH611
A	HOH686
B	TYR103

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 304

Chain	Residue
A	ALA78
A	TYR206
B	TYR197

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 305

Chain	Residue
A	HIS12
A	GLN17
A	ASN58
A	ASP60
A	HOH435

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 306

Chain	Residue
A	ASP8
A	ASP9
A	SER39
A	ASN92
A	HOH414
A	HOH416

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 B 301

Chain	Residue
B	ASN96
B	ASP100
B	MPD305
B	HOH419
B	HOH432
B	HOH559
B	HOH663
B	HOH664

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 302

Chain	Residue
B	ASP8
B	ASP9
B	SER39
B	ASN92
B	HOH417
B	HOH419

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 303

Chain	Residue
B	GLY200
B	PRO201
B	HOH659
D	ARG192

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD B 304

Chain	Residue
B	ARG192
B	HOH660
B	HOH661
D	ILE199
D	GLY200

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MPD B 305

Chain	Residue
B	ASP100
B	TYR103
B	ILE199
B	GLY200
B	PRO202
B	PO4301
B	HOH450
B	HOH492
B	HOH659
B	HOH665

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MPD B 306

Chain	Residue
A	TYR103
A	ALA182
A	HOH562
B	TYR73
B	VAL76
B	ASN77
B	ALA112
B	HOH486

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 301

Chain	Residue
C	ASN96
C	ASP100
C	MPD305
C	HOH460
C	HOH495
C	HOH507
C	HOH528

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 302

Chain	Residue
C	ASP8
C	ASP9
C	SER39
C	ASN92
C	HOH507
C	HOH565

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 303

Chain	Residue
C	TYR73
C	ASN77
C	ALA112
C	HOH458
D	TYR103
D	ALA182

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 304

Chain	Residue
D	ALA112
C	TYR103
C	ALA182
C	HOH452
D	ASN77

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD C 305

Chain	Residue
C	ASP100
C	TYR103
C	PRO202
C	PO4301
C	HOH435
C	HOH576

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 D 301

Chain	Residue
C	LEU47
D	ASN96
D	ASP100
D	HOH418
D	HOH421
D	HOH574
D	HOH595
D	HOH601

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 302

Chain	Residue
D	ASP8
D	ASP9
D	SER39
D	ASN92
D	HOH417
D	HOH418

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 303

Chain	Residue
D	HIS12
D	ASN58
D	ASP60
D	HOH513

site_id	CC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MPD D 304

Chain	Residue
C	TYR73
D	ASP100
D	ALA182
D	ILE199
D	GLY200
D	PRO201
D	PRO202
D	HOH405

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

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