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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
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0016853molecular_functionisomerase activity
A0061593molecular_functionsulfoquinovose isomerase activity
A0061720biological_process6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
A1902777biological_process6-sulfoquinovose(1-) catabolic process
B0005975biological_processcarbohydrate metabolic process
B0016853molecular_functionisomerase activity
B0061593molecular_functionsulfoquinovose isomerase activity
B0061720biological_process6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
B1902777biological_process6-sulfoquinovose(1-) catabolic process
C0005975biological_processcarbohydrate metabolic process
C0016853molecular_functionisomerase activity
C0061593molecular_functionsulfoquinovose isomerase activity
C0061720biological_process6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
C1902777biological_process6-sulfoquinovose(1-) catabolic process
D0005975biological_processcarbohydrate metabolic process
D0016853molecular_functionisomerase activity
D0061593molecular_functionsulfoquinovose isomerase activity
D0061720biological_process6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
D1902777biological_process6-sulfoquinovose(1-) catabolic process
E0005975biological_processcarbohydrate metabolic process
E0016853molecular_functionisomerase activity
E0061593molecular_functionsulfoquinovose isomerase activity
E0061720biological_process6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
E1902777biological_process6-sulfoquinovose(1-) catabolic process
F0005975biological_processcarbohydrate metabolic process
F0016853molecular_functionisomerase activity
F0061593molecular_functionsulfoquinovose isomerase activity
F0061720biological_process6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde
F1902777biological_process6-sulfoquinovose(1-) catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue RB8 A 501
ChainResidue
ATRP51
AGLN362
ATRP375
AGLN379
AASP380
AHIS383
AHOH647
AHOH670
AHOH674
AARG55
ATYR111
AASN172
AHIS176
AARG238
APHE239
AGLU251
ATRP316

site_idAC2
Number of Residues17
Detailsbinding site for residue RB8 B 501
ChainResidue
BTRP51
BARG55
BTYR111
BASN172
BMET175
BHIS176
BARG238
BPHE239
BGLU251
BTRP316
BGLN362
BTRP375
BGLN379
BASP380
BHIS383
BHOH646
BHOH658

site_idAC3
Number of Residues17
Detailsbinding site for residue RB8 D 501
ChainResidue
DTRP51
DARG55
DTYR111
DASN172
DMET175
DHIS176
DARG238
DPHE239
DGLU251
DTRP316
DGLN362
DTRP375
DGLN379
DASP380
DHIS383
DHOH612
DHOH613

site_idAC4
Number of Residues13
Detailsbinding site for residue RB8 F 501
ChainResidue
FTRP51
FARG55
FASN172
FMET175
FHIS176
FGLU251
FTRP316
FGLN362
FGLN379
FASP380
FHIS383
FHOH604
FHOH616

site_idAC5
Number of Residues17
Detailsbinding site for residue RB8 C 501
ChainResidue
CTRP51
CARG55
CTYR111
CASN172
CMET175
CHIS176
CARG238
CPHE239
CGLU251
CTRP316
CGLN362
CTRP375
CGLN379
CASP380
CHIS383
CHOH642
CHOH681

site_idAC6
Number of Residues14
Detailsbinding site for residue RB8 E 501
ChainResidue
ETRP51
EARG55
ETYR111
EASN172
EMET175
EHIS176
EGLU251
ETRP316
EGLN362
EGLN379
EASP380
EHIS383
EHOH608
EHOH625

Functional Information from PROSITE/UniProt
site_idPS01295
Number of Residues8
DetailsISPD 4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature. VIIHDVAR
ChainResidueDetails
AVAL203-ARG210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00998","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18328504","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"33791429","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues34
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00998","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18328504","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"33791429","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7AG4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00998","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33791429","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7AG4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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