Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4HX9

Designed Phosphodeoxyribosyltransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009117	biological_process	nucleotide metabolic process
A	0016740	molecular_function	transferase activity
A	0043173	biological_process	nucleotide salvage
A	0050144	molecular_function	nucleoside deoxyribosyltransferase activity
B	0009117	biological_process	nucleotide metabolic process
B	0016740	molecular_function	transferase activity
B	0043173	biological_process	nucleotide salvage
B	0050144	molecular_function	nucleoside deoxyribosyltransferase activity
C	0009117	biological_process	nucleotide metabolic process
C	0016740	molecular_function	transferase activity
C	0043173	biological_process	nucleotide salvage
C	0050144	molecular_function	nucleoside deoxyribosyltransferase activity
D	0009117	biological_process	nucleotide metabolic process
D	0016740	molecular_function	transferase activity
D	0043173	biological_process	nucleotide salvage
D	0050144	molecular_function	nucleoside deoxyribosyltransferase activity
E	0009117	biological_process	nucleotide metabolic process
E	0016740	molecular_function	transferase activity
E	0043173	biological_process	nucleotide salvage
E	0050144	molecular_function	nucleoside deoxyribosyltransferase activity
F	0009117	biological_process	nucleotide metabolic process
F	0016740	molecular_function	transferase activity
F	0043173	biological_process	nucleotide salvage
F	0050144	molecular_function	nucleoside deoxyribosyltransferase activity
G	0009117	biological_process	nucleotide metabolic process
G	0016740	molecular_function	transferase activity
G	0043173	biological_process	nucleotide salvage
G	0050144	molecular_function	nucleoside deoxyribosyltransferase activity
H	0009117	biological_process	nucleotide metabolic process
H	0016740	molecular_function	transferase activity
H	0043173	biological_process	nucleotide salvage
H	0050144	molecular_function	nucleoside deoxyribosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 201

Chain	Residue
A	ILE34
A	ASP35
A	LEU36
A	GLU37

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 202

Chain	Residue
B	GLY94
B	LEU95
B	GLY96
A	GLY92
A	THR93
A	GLY94
A	GLY96
B	THR93

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PG4 A 203

Chain	Residue
A	THR66
A	ASN70
A	TRP127
A	GLY128
A	SER130
A	PHE149
B	ASN70
B	TRP127
B	PHE149
B	PHE151

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 201

Chain	Residue
B	ILE34
B	LEU36
B	GLU37
B	HOH302
B	HOH331

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PG4 B 202

Chain	Residue
B	TYR118
B	GLU153
B	HOH340

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 201

Chain	Residue
E	ILE34
E	LEU36
E	GLU37

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 202

Chain	Residue
E	GLN91
E	GLY92
E	GLY94
E	LEU95

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 F 201

Chain	Residue
A	LYS22
A	GLU26
F	ILE34
F	ASP35
F	LEU36
F	GLU37
F	HOH301

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 F 202

Chain	Residue
E	TYR157
F	GLN17
F	GLN91
F	GLY92
F	THR93
F	GLY94
F	LEU95

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 F 203

Chain	Residue
A	TYR58
A	ASP61
F	TYR118
F	GLY119
F	LYS120
F	GLU153

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 F 204

Chain	Residue
C	TRP127
C	PHE149
D	ASN70
E	ASN70
F	TRP127
F	PHE149

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 201

Chain	Residue
C	LYS29
C	ILE34
C	LEU36
C	GLU37

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 201

Chain	Residue
D	ILE34
D	ASP35
D	LEU36
D	GLU37
D	HOH309

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 202

Chain	Residue
D	GLN17
D	GLY92
D	THR93
D	GLY94
D	LEU95
D	HOH324

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PG4 D 203

Chain	Residue
C	ASP61
D	ASP115
D	GLU116
D	TYR118

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PG4 D 204

Chain	Residue
C	ASN70
D	TRP127
D	GLY128
D	SER130
D	PHE149
D	PHE151
G	TRP127
G	GLY128
G	PHE149
H	THR66
H	ASN70

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 G 201

Chain	Residue
G	LEU95
G	HOH306
H	TYR157
G	ARG13
G	GLN17
G	GLN91
G	GLY92
G	THR93
G	GLY94

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 G 202

Chain	Residue
G	ILE34
G	ASP35
G	LEU36
G	GLU37

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 H 201

Chain	Residue
H	ILE34
H	ASP35
H	LEU36
H	GLU37

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 H 202

Chain	Residue
G	TYR157
H	ARG13
H	GLN91
H	GLY92
H	GLY94
H	LEU95

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"7797550","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 554

Chain	Residue	Details
A	TYR7	electrostatic stabiliser
A	ASP72	electrostatic stabiliser
A	GLY92	proton donor, proton shuttle (general acid/base)
A	GLU98	covalently attached, electrostatic stabiliser

site_id	MCSA2
Number of Residues	3
Details	M-CSA 554

Chain	Residue	Details
B	TYR7	electrostatic stabiliser
B	ASP72	electrostatic stabiliser
B	GLU98	covalently attached, electrostatic stabiliser

site_id	MCSA3
Number of Residues	4
Details	M-CSA 554

Chain	Residue	Details
C	TYR7	electrostatic stabiliser
C	ASP72	electrostatic stabiliser
C	GLY92	proton donor, proton shuttle (general acid/base)
C	GLU98	covalently attached, electrostatic stabiliser

site_id	MCSA4
Number of Residues	4
Details	M-CSA 554

Chain	Residue	Details
D	TYR7	electrostatic stabiliser
D	ASP72	electrostatic stabiliser
D	GLY92	proton donor, proton shuttle (general acid/base)
D	GLU98	covalently attached, electrostatic stabiliser

site_id	MCSA5
Number of Residues	4
Details	M-CSA 554

Chain	Residue	Details
E	TYR7	electrostatic stabiliser
E	ASP72	electrostatic stabiliser
E	GLY92	proton donor, proton shuttle (general acid/base)
E	GLU98	covalently attached, electrostatic stabiliser

site_id	MCSA6
Number of Residues	4
Details	M-CSA 554

Chain	Residue	Details
F	TYR7	electrostatic stabiliser
F	ASP72	electrostatic stabiliser
F	GLY92	proton donor, proton shuttle (general acid/base)
F	GLU98	covalently attached, electrostatic stabiliser

site_id	MCSA7
Number of Residues	4
Details	M-CSA 554

Chain	Residue	Details
G	TYR7	electrostatic stabiliser
G	ASP72	electrostatic stabiliser
G	GLY92	proton donor, proton shuttle (general acid/base)
G	GLU98	covalently attached, electrostatic stabiliser

site_id	MCSA8
Number of Residues	4
Details	M-CSA 554

Chain	Residue	Details
H	TYR7	electrostatic stabiliser
H	ASP72	electrostatic stabiliser
H	GLY92	proton donor, proton shuttle (general acid/base)
H	GLU98	covalently attached, electrostatic stabiliser

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