Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7AG4

Crystal structure of active site mutant of SQ Isomerase (YihS-H248A) from Salmonella enterica in complex with sulfofructose (SF)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005975	biological_process	carbohydrate metabolic process
A	0016853	molecular_function	isomerase activity
A	0061593	molecular_function	sulfoquinovose isomerase activity
A	0061720	biological_process	6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
A	1902777	biological_process	6-sulfoquinovose(1-) catabolic process
B	0005975	biological_process	carbohydrate metabolic process
B	0016853	molecular_function	isomerase activity
B	0061593	molecular_function	sulfoquinovose isomerase activity
B	0061720	biological_process	6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
B	1902777	biological_process	6-sulfoquinovose(1-) catabolic process
C	0005975	biological_process	carbohydrate metabolic process
C	0016853	molecular_function	isomerase activity
C	0061593	molecular_function	sulfoquinovose isomerase activity
C	0061720	biological_process	6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
C	1902777	biological_process	6-sulfoquinovose(1-) catabolic process
D	0005975	biological_process	carbohydrate metabolic process
D	0016853	molecular_function	isomerase activity
D	0061593	molecular_function	sulfoquinovose isomerase activity
D	0061720	biological_process	6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
D	1902777	biological_process	6-sulfoquinovose(1-) catabolic process
E	0005975	biological_process	carbohydrate metabolic process
E	0016853	molecular_function	isomerase activity
E	0061593	molecular_function	sulfoquinovose isomerase activity
E	0061720	biological_process	6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
E	1902777	biological_process	6-sulfoquinovose(1-) catabolic process
F	0005975	biological_process	carbohydrate metabolic process
F	0016853	molecular_function	isomerase activity
F	0061593	molecular_function	sulfoquinovose isomerase activity
F	0061720	biological_process	6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
F	1902777	biological_process	6-sulfoquinovose(1-) catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue RB8 A 501

Chain	Residue
A	TRP51
A	GLN362
A	TRP375
A	GLN379
A	ASP380
A	HIS383
A	HOH647
A	HOH670
A	HOH674
A	ARG55
A	TYR111
A	ASN172
A	HIS176
A	ARG238
A	PHE239
A	GLU251
A	TRP316

site_id	AC2
Number of Residues	17
Details	binding site for residue RB8 B 501

Chain	Residue
B	TRP51
B	ARG55
B	TYR111
B	ASN172
B	MET175
B	HIS176
B	ARG238
B	PHE239
B	GLU251
B	TRP316
B	GLN362
B	TRP375
B	GLN379
B	ASP380
B	HIS383
B	HOH646
B	HOH658

site_id	AC3
Number of Residues	17
Details	binding site for residue RB8 D 501

Chain	Residue
D	TRP51
D	ARG55
D	TYR111
D	ASN172
D	MET175
D	HIS176
D	ARG238
D	PHE239
D	GLU251
D	TRP316
D	GLN362
D	TRP375
D	GLN379
D	ASP380
D	HIS383
D	HOH612
D	HOH613

site_id	AC4
Number of Residues	13
Details	binding site for residue RB8 F 501

Chain	Residue
F	TRP51
F	ARG55
F	ASN172
F	MET175
F	HIS176
F	GLU251
F	TRP316
F	GLN362
F	GLN379
F	ASP380
F	HIS383
F	HOH604
F	HOH616

site_id	AC5
Number of Residues	17
Details	binding site for residue RB8 C 501

Chain	Residue
C	TRP51
C	ARG55
C	TYR111
C	ASN172
C	MET175
C	HIS176
C	ARG238
C	PHE239
C	GLU251
C	TRP316
C	GLN362
C	TRP375
C	GLN379
C	ASP380
C	HIS383
C	HOH642
C	HOH681

site_id	AC6
Number of Residues	14
Details	binding site for residue RB8 E 501

Chain	Residue
E	TRP51
E	ARG55
E	TYR111
E	ASN172
E	MET175
E	HIS176
E	GLU251
E	TRP316
E	GLN362
E	GLN379
E	ASP380
E	HIS383
E	HOH608
E	HOH625

Functional Information from PROSITE/UniProt

site_id	PS01295
Number of Residues	8
Details	ISPD 4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature. VIIHDVAR

Chain	Residue	Details
A	VAL203-ARG210

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_00998, ECO:0000305\|PubMed:18328504, ECO:0000305\|PubMed:33791429

Chain	Residue	Details
A	ALA248
C	HIS383
E	ALA248
E	HIS383
A	HIS383
B	ALA248
B	HIS383
D	ALA248
D	HIS383
F	ALA248
F	HIS383
C	ALA248

site_id	SWS_FT_FI2
Number of Residues	36
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00998, ECO:0000305\|PubMed:18328504, ECO:0000305\|PubMed:33791429, ECO:0007744\|PDB:7AG4

Chain	Residue	Details
A	ARG55
B	HIS176
B	ARG238
B	GLU251
D	ARG55
D	TYR111
D	ASN172
D	HIS176
D	ARG238
D	GLU251
F	ARG55
A	TYR111
F	TYR111
F	ASN172
F	HIS176
F	ARG238
F	GLU251
C	ARG55
C	TYR111
C	ASN172
C	HIS176
C	ARG238
A	ASN172
C	GLU251
E	ARG55
E	TYR111
E	ASN172
E	HIS176
E	ARG238
E	GLU251
A	HIS176
A	ARG238
A	GLU251
B	ARG55
B	TYR111
B	ASN172

site_id	SWS_FT_FI3
Number of Residues	18
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00998, ECO:0000305\|PubMed:33791429, ECO:0007744\|PDB:7AG4

Chain	Residue	Details
A	GLN362
F	GLN362
F	GLN379
F	HIS383
C	GLN362
C	GLN379
C	HIS383
E	GLN362
E	GLN379
E	HIS383
A	GLN379
A	HIS383
B	GLN362
B	GLN379
B	HIS383
D	GLN362
D	GLN379
D	HIS383

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