Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6MSW

Crystal structure of BH1352 2-deoxyribose-5-phosphate from Bacillus halodurans, K184L mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004139	molecular_function	deoxyribose-phosphate aldolase activity
A	0005737	cellular_component	cytoplasm
A	0006018	biological_process	2-deoxyribose 1-phosphate catabolic process
A	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
A	0009264	biological_process	deoxyribonucleotide catabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0016829	molecular_function	lyase activity
A	0046386	biological_process	deoxyribose phosphate catabolic process
B	0003824	molecular_function	catalytic activity
B	0004139	molecular_function	deoxyribose-phosphate aldolase activity
B	0005737	cellular_component	cytoplasm
B	0006018	biological_process	2-deoxyribose 1-phosphate catabolic process
B	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
B	0009264	biological_process	deoxyribonucleotide catabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0016829	molecular_function	lyase activity
B	0046386	biological_process	deoxyribose phosphate catabolic process
C	0003824	molecular_function	catalytic activity
C	0004139	molecular_function	deoxyribose-phosphate aldolase activity
C	0005737	cellular_component	cytoplasm
C	0006018	biological_process	2-deoxyribose 1-phosphate catabolic process
C	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
C	0009264	biological_process	deoxyribonucleotide catabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0016829	molecular_function	lyase activity
C	0046386	biological_process	deoxyribose phosphate catabolic process
D	0003824	molecular_function	catalytic activity
D	0004139	molecular_function	deoxyribose-phosphate aldolase activity
D	0005737	cellular_component	cytoplasm
D	0006018	biological_process	2-deoxyribose 1-phosphate catabolic process
D	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
D	0009264	biological_process	deoxyribonucleotide catabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0016829	molecular_function	lyase activity
D	0046386	biological_process	deoxyribose phosphate catabolic process
E	0003824	molecular_function	catalytic activity
E	0004139	molecular_function	deoxyribose-phosphate aldolase activity
E	0005737	cellular_component	cytoplasm
E	0006018	biological_process	2-deoxyribose 1-phosphate catabolic process
E	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
E	0009264	biological_process	deoxyribonucleotide catabolic process
E	0016052	biological_process	carbohydrate catabolic process
E	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
E	0016829	molecular_function	lyase activity
E	0046386	biological_process	deoxyribose phosphate catabolic process
F	0003824	molecular_function	catalytic activity
F	0004139	molecular_function	deoxyribose-phosphate aldolase activity
F	0005737	cellular_component	cytoplasm
F	0006018	biological_process	2-deoxyribose 1-phosphate catabolic process
F	0006207	biological_process	'de novo' pyrimidine nucleobase biosynthetic process
F	0009264	biological_process	deoxyribonucleotide catabolic process
F	0016052	biological_process	carbohydrate catabolic process
F	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
F	0016829	molecular_function	lyase activity
F	0046386	biological_process	deoxyribose phosphate catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue GOL A 301

Chain	Residue
A	LYS148
A	ALA149
F	VAL147
F	LYS148

site_id	AC2
Number of Residues	4
Details	binding site for residue GOL A 302

Chain	Residue
A	GLU28
A	LYS31
A	SER193
A	ASP194

site_id	AC3
Number of Residues	1
Details	binding site for residue GOL A 303

Chain	Residue
D	GLU20

site_id	AC4
Number of Residues	4
Details	binding site for residue GOL B 302

Chain	Residue
B	GLN113
B	GLU120
B	LYS148
E	VAL147

site_id	AC5
Number of Residues	3
Details	binding site for residue GOL B 303

Chain	Residue
B	GLU28
B	GLU32
B	ASP194

site_id	AC6
Number of Residues	2
Details	binding site for residue GOL C 301

Chain	Residue
B	GLU20
C	GLU32

site_id	AC7
Number of Residues	2
Details	binding site for residue GOL C 303

Chain	Residue
C	ASP191
C	ASP194

site_id	AC8
Number of Residues	4
Details	binding site for residue GOL D 301

Chain	Residue
C	GLU120
C	ALA149
D	VAL147
D	LYS148

site_id	AC9
Number of Residues	5
Details	binding site for residue GOL D 302

Chain	Residue
C	VAL147
C	LYS148
D	GLN113
D	LYS148
D	HOH425

site_id	AD1
Number of Residues	1
Details	binding site for residue GOL D 303

Chain	Residue
D	LEU145

site_id	AD2
Number of Residues	3
Details	binding site for residue GOL D 304

Chain	Residue
D	ASP191
D	ASP194
D	HOH408

site_id	AD3
Number of Residues	4
Details	binding site for residue GOL E 301

Chain	Residue
B	VAL147
B	LYS148
E	GLU120
E	ALA149

site_id	AD4
Number of Residues	1
Details	binding site for residue GOL E 302

Chain	Residue
E	GLU144

site_id	AD5
Number of Residues	4
Details	binding site for residue GOL F 301

Chain	Residue
A	VAL147
A	LYS148
F	GLU120
F	ALA149

site_id	AD6
Number of Residues	2
Details	binding site for residue GOL F 302

Chain	Residue
F	ILE84
F	GLU85

Functional Information from PROSITE/UniProt

site_id	PS00912
Number of Residues	21
Details	DHODEHASE_2 Dihydroorotate dehydrogenase signature 2. VLAsGGVrDlsdAkaMIdAGA

Chain	Residue	Details
A	VAL183-ALA203

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_00114

Chain	Residue	Details
A	ASP92
E	LEU184
F	ASP92
F	LEU184
A	LEU184
B	ASP92
B	LEU184
C	ASP92
C	LEU184
D	ASP92
D	LEU184
E	ASP92

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: Schiff-base intermediate with acetaldehyde => ECO:0000255\|HAMAP-Rule:MF_00114

Chain	Residue	Details
A	LYS155
B	LYS155
C	LYS155
D	LYS155
E	LYS155
F	LYS155

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