Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4TTJ

Crystal structure of double mutant E. Coli purine nucleoside phosphorylase with 6 FMC molecules

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004731	molecular_function	purine-nucleoside phosphorylase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006152	biological_process	purine nucleoside catabolic process
A	0006974	biological_process	DNA damage response
A	0009116	biological_process	nucleoside metabolic process
A	0009164	biological_process	nucleoside catabolic process
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0019686	biological_process	purine nucleoside interconversion
A	0042278	biological_process	purine nucleoside metabolic process
A	0042802	molecular_function	identical protein binding
A	0047975	molecular_function	guanosine phosphorylase activity
B	0003824	molecular_function	catalytic activity
B	0004731	molecular_function	purine-nucleoside phosphorylase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006152	biological_process	purine nucleoside catabolic process
B	0006974	biological_process	DNA damage response
B	0009116	biological_process	nucleoside metabolic process
B	0009164	biological_process	nucleoside catabolic process
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0019686	biological_process	purine nucleoside interconversion
B	0042278	biological_process	purine nucleoside metabolic process
B	0042802	molecular_function	identical protein binding
B	0047975	molecular_function	guanosine phosphorylase activity
D	0003824	molecular_function	catalytic activity
D	0004731	molecular_function	purine-nucleoside phosphorylase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006152	biological_process	purine nucleoside catabolic process
D	0006974	biological_process	DNA damage response
D	0009116	biological_process	nucleoside metabolic process
D	0009164	biological_process	nucleoside catabolic process
D	0016020	cellular_component	membrane
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0016763	molecular_function	pentosyltransferase activity
D	0019686	biological_process	purine nucleoside interconversion
D	0042278	biological_process	purine nucleoside metabolic process
D	0042802	molecular_function	identical protein binding
D	0047975	molecular_function	guanosine phosphorylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue PO4 A 301

Chain	Residue
A	PRO19
A	GLY20
A	ARG24
A	ARG87
A	GLY89
A	SER90
A	FMC302
D	ARG43

site_id	AC2
Number of Residues	18
Details	binding site for residue FMC A 302

Chain	Residue
A	ARG87
A	SER90
A	CYS91
A	GLY92
A	PHE159
A	VAL178
A	GLU179
A	MET180
A	GLU181
A	SER203
A	PO4301
A	HOH537
A	HOH584
A	HOH634
A	HOH684
D	HIS4
D	ARG43
A	MET64

site_id	AC3
Number of Residues	6
Details	binding site for residue SO4 A 303

Chain	Residue
A	ASN222
A	ASP223
A	HOH527
A	HOH533
A	HOH564
A	HOH637

site_id	AC4
Number of Residues	8
Details	binding site for residue PO4 B 301

Chain	Residue
B	GLY20
B	ARG43
B	ARG87
B	GLY89
B	SER90
B	FMC302
B	HOH401
B	HOH403

site_id	AC5
Number of Residues	17
Details	binding site for residue FMC B 302

Chain	Residue
B	HIS4
B	ARG43
B	MET64
B	ARG87
B	SER90
B	CYS91
B	GLY92
B	PHE159
B	VAL178
B	GLU179
B	MET180
B	GLU181
B	ILE206
B	PO4301
B	HOH434
B	HOH559
B	HOH584

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 B 303

Chain	Residue
B	LYS99
B	LEU100
B	HIS205
B	GLU210

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 B 304

Chain	Residue
B	GLN218
B	THR219
B	ASN222

site_id	AC8
Number of Residues	8
Details	binding site for residue PO4 D 301

Chain	Residue
A	ARG43
D	GLY20
D	ARG87
D	GLY89
D	SER90
D	FMC302
D	HOH461
D	HOH600

site_id	AC9
Number of Residues	15
Details	binding site for residue FMC D 302

Chain	Residue
A	HIS4
A	ARG43
D	MET64
D	ARG87
D	SER90
D	CYS91
D	GLY92
D	PHE159
D	VAL178
D	GLU179
D	MET180
D	GLU181
D	PO4301
D	HOH569
D	HOH679

Functional Information from PROSITE/UniProt

site_id	PS01232
Number of Residues	16
Details	PNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL

Chain	Residue	Details
A	GLY61-LEU76

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4TS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	15
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"11786017","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21672603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OOE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OOH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OPV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11786017","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21672603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OOE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OOH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OPV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	9
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4TS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TS9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TTJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21672603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30337572","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 375

Chain	Residue	Details
A	GLY20	electrostatic stabiliser
A	ARG24	electrostatic stabiliser
A	ARG43	electrostatic stabiliser
A	ARG87	electrostatic stabiliser
A	SER90	electrostatic stabiliser
A	ALA204	proton shuttle (general acid/base)
A	ALA217	enhance reactivity

site_id	MCSA2
Number of Residues	7
Details	M-CSA 375

Chain	Residue	Details
B	GLY20	electrostatic stabiliser
B	ARG24	electrostatic stabiliser
B	ARG43	electrostatic stabiliser
B	ARG87	electrostatic stabiliser
B	SER90	electrostatic stabiliser
B	ALA204	proton shuttle (general acid/base)
B	ALA217	enhance reactivity

site_id	MCSA3
Number of Residues	7
Details	M-CSA 375

Chain

Residue

Details

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