Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1HPU

5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0008252	molecular_function	nucleotidase activity
A	0008253	molecular_function	5'-nucleotidase activity
A	0008768	molecular_function	UDP-sugar diphosphatase activity
A	0009166	biological_process	nucleotide catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0106411	molecular_function	XMP 5'-nucleosidase activity
B	0000166	molecular_function	nucleotide binding
B	0008252	molecular_function	nucleotidase activity
B	0008253	molecular_function	5'-nucleotidase activity
B	0008768	molecular_function	UDP-sugar diphosphatase activity
B	0009166	biological_process	nucleotide catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
B	0106411	molecular_function	XMP 5'-nucleosidase activity
C	0000166	molecular_function	nucleotide binding
C	0008252	molecular_function	nucleotidase activity
C	0008253	molecular_function	5'-nucleotidase activity
C	0008768	molecular_function	UDP-sugar diphosphatase activity
C	0009166	biological_process	nucleotide catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016788	molecular_function	hydrolase activity, acting on ester bonds
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
C	0106411	molecular_function	XMP 5'-nucleosidase activity
D	0000166	molecular_function	nucleotide binding
D	0008252	molecular_function	nucleotidase activity
D	0008253	molecular_function	5'-nucleotidase activity
D	0008768	molecular_function	UDP-sugar diphosphatase activity
D	0009166	biological_process	nucleotide catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016788	molecular_function	hydrolase activity, acting on ester bonds
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0042597	cellular_component	periplasmic space
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	7
Details	BINDING SITE FOR RESIDUE MN A 600

Chain	Residue
A	ASP84
A	ASN116
A	HIS217
A	HIS252
A	MN601
A	A121602
A	HOH1669

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN A 601

Chain	Residue
A	ASP84
A	GLN254
A	MN600
A	A121602
A	HOH1669
A	ASP41
A	HIS43

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN B 600

Chain	Residue
B	ASP84
B	ASN116
B	HIS217
B	HIS252
B	MN601
B	A121603
B	HOH1690

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN B 601

Chain	Residue
B	ASP41
B	HIS43
B	ASP84
B	GLN254
B	MN600
B	A121603
B	HOH1690

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN C 600

Chain	Residue
C	ASP84
C	ASN116
C	HIS217
C	HIS252
C	MN601
C	A121604
C	HOH1681

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN C 601

Chain	Residue
C	ASP41
C	HIS43
C	ASP84
C	GLN254
C	MN600
C	HOH1681
C	HOH1885

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN D 600

Chain	Residue
D	ASP84
D	ASN116
D	HIS217
D	HIS252
D	MN601
D	A121605
D	HOH1652

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN D 601

Chain	Residue
D	ASP41
D	HIS43
D	ASP84
D	GLN254
D	MN600
D	HOH1652
D	HOH1812

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE A12 A 1602

Chain	Residue
A	ASP84
A	ASN116
A	HIS117
A	ASP120
A	ILE178
A	HIS252
A	GLN254
A	ARG375
A	ARG379
A	SER405
A	GLY407
A	ARG410
A	PHE429
A	ASN431
A	GLY458
A	PHE498
A	ASP504
A	MN600
A	MN601
A	HOH1631
A	HOH1633
A	HOH1669
A	HOH1673
A	HOH1742

site_id	BC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE A12 B 1603

Chain	Residue
B	HOH1690
B	HOH1702
B	HOH1719
B	HOH1738
B	HOH1768
B	HOH1905
B	ASP84
B	ASN116
B	HIS117
B	ASP120
B	ILE178
B	HIS252
B	GLN254
B	ARG375
B	ARG379
B	SER405
B	GLY407
B	ARG410
B	PHE429
B	ASN431
B	GLY458
B	PHE498
B	ASP504
B	MN600
B	MN601

site_id	BC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE A12 C 1604

Chain	Residue
C	ASP84
C	ASN116
C	HIS117
C	ILE178
C	HIS252
C	ARG375
C	ARG379
C	SER405
C	GLY407
C	ARG410
C	PHE429
C	ASN431
C	GLY458
C	PHE498
C	ASP504
C	MN600
C	HOH1679
C	HOH1681
C	HOH1693
C	HOH1795
C	HOH1797
C	HOH1808
C	HOH1885

site_id	BC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE A12 D 1605

Chain	Residue
D	ASP84
D	ASN116
D	HIS117
D	ILE178
D	HIS252
D	ARG375
D	ARG379
D	SER405
D	GLY407
D	ARG410
D	PHE429
D	ASN431
D	GLY458
D	PHE498
D	ASP504
D	MN600
D	HOH1652
D	HOH1771
D	HOH1812
D	HOH1824
D	HOH1835
D	HOH1864

Functional Information from PROSITE/UniProt

site_id	PS00785
Number of Residues	13
Details	5_NUCLEOTIDASE_1 5'-nucleotidase signature 1. ItVLHTnDhHGhF

Chain	Residue	Details
A	ILE34-PHE46

site_id	PS00786
Number of Residues	12
Details	5_NUCLEOTIDASE_2 5'-nucleotidase signature 2. YdamaIGNHEFD

Chain	Residue	Details
A	TYR109-ASP120

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING:

Chain	Residue	Details
A	ASP41
B	ASP41
B	HIS43
B	ASP84
B	ASN116
B	HIS217
B	HIS252
B	GLN254
B	ARG375
B	PHE498
C	ASP41
A	HIS43
C	HIS43
C	ASP84
C	ASN116
C	HIS217
C	HIS252
C	GLN254
C	ARG375
C	PHE498
D	ASP41
D	HIS43
A	ASP84
D	ASP84
D	ASN116
D	HIS217
D	HIS252
D	GLN254
D	ARG375
D	PHE498
A	ASN116
A	HIS217
A	HIS252
A	GLN254
A	ARG375
A	PHE498

site_id	SWS_FT_FI2
Number of Residues	8
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	HIS117
A	ASP120
B	HIS117
B	ASP120
C	HIS117
C	ASP120
D	HIS117
D	ASP120

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1ush

Chain	Residue	Details
A	ARG375
A	ARG410
A	ASP120
A	HIS117
A	ARG379
A	ASN116

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1ush

Chain	Residue	Details
B	ARG375
B	ARG410
B	ASP120
B	HIS117
B	ARG379
B	ASN116

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1ush

Chain	Residue	Details
C	ARG375
C	ARG410
C	ASP120
C	HIS117
C	ARG379
C	ASN116

site_id	CSA4
Number of Residues	6
Details	Annotated By Reference To The Literature 1ush

Chain	Residue	Details
D	ARG375
D	ARG410
D	ASP120
D	HIS117
D	ARG379
D	ASN116

site_id	MCSA1
Number of Residues	12
Details	M-CSA 611

Chain	Residue	Details
A	ASP41	metal ligand
A	ARG375	electrostatic stabiliser, increase acidity, increase electrophilicity
A	ARG379	electrostatic stabiliser, increase acidity, increase electrophilicity
A	ARG410	electrostatic stabiliser, increase acidity, increase electrophilicity
A	HIS43	metal ligand
A	ASP84	metal ligand
A	ASN116	electrostatic stabiliser, metal ligand
A	HIS117	electrostatic stabiliser, increase nucleophilicity, metal ligand, proton acceptor
A	ASP120	electrostatic stabiliser, increase basicity
A	HIS217	metal ligand
A	HIS252	metal ligand
A	GLN254	metal ligand

site_id	MCSA2
Number of Residues	12
Details	M-CSA 611

Chain	Residue	Details
B	ASP41	metal ligand
B	ARG375	electrostatic stabiliser, increase acidity, increase electrophilicity
B	ARG379	electrostatic stabiliser, increase acidity, increase electrophilicity
B	ARG410	electrostatic stabiliser, increase acidity, increase electrophilicity
B	HIS43	metal ligand
B	ASP84	metal ligand
B	ASN116	electrostatic stabiliser, metal ligand
B	HIS117	electrostatic stabiliser, increase nucleophilicity, metal ligand, proton acceptor
B	ASP120	electrostatic stabiliser, increase basicity
B	HIS217	metal ligand
B	HIS252	metal ligand
B	GLN254	metal ligand

site_id	MCSA3
Number of Residues	12
Details	M-CSA 611

Chain	Residue	Details
C	ASP41	metal ligand
C	ARG375	electrostatic stabiliser, increase acidity, increase electrophilicity
C	ARG379	electrostatic stabiliser, increase acidity, increase electrophilicity
C	ARG410	electrostatic stabiliser, increase acidity, increase electrophilicity
C	HIS43	metal ligand
C	ASP84	metal ligand
C	ASN116	electrostatic stabiliser, metal ligand
C	HIS117	electrostatic stabiliser, increase nucleophilicity, metal ligand, proton acceptor
C	ASP120	electrostatic stabiliser, increase basicity
C	HIS217	metal ligand
C	HIS252	metal ligand
C	GLN254	metal ligand

site_id	MCSA4
Number of Residues	12
Details	M-CSA 611

Chain	Residue	Details
D	ASP41	metal ligand
D	ARG375	electrostatic stabiliser, increase acidity, increase electrophilicity
D	ARG379	electrostatic stabiliser, increase acidity, increase electrophilicity
D	ARG410	electrostatic stabiliser, increase acidity, increase electrophilicity
D	HIS43	metal ligand
D	ASP84	metal ligand
D	ASN116	electrostatic stabiliser, metal ligand
D	HIS117	electrostatic stabiliser, increase nucleophilicity, metal ligand, proton acceptor
D	ASP120	electrostatic stabiliser, increase basicity
D	HIS217	metal ligand
D	HIS252	metal ligand
D	GLN254	metal ligand

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