Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7AG7

Crystal structure of SFP aldolase YihT from Salmonella enterica in complex with sulfate bound at the active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
A1902777biological_process6-sulfoquinovose(1-) catabolic process
B0016829molecular_functionlyase activity
B0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
B1902777biological_process6-sulfoquinovose(1-) catabolic process
C0016829molecular_functionlyase activity
C0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
C1902777biological_process6-sulfoquinovose(1-) catabolic process
D0016829molecular_functionlyase activity
D0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
D1902777biological_process6-sulfoquinovose(1-) catabolic process
E0016829molecular_functionlyase activity
E0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
E1902777biological_process6-sulfoquinovose(1-) catabolic process
F0016829molecular_functionlyase activity
F0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
F1902777biological_process6-sulfoquinovose(1-) catabolic process
G0016829molecular_functionlyase activity
G0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
G1902777biological_process6-sulfoquinovose(1-) catabolic process
H0016829molecular_functionlyase activity
H0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
H1902777biological_process6-sulfoquinovose(1-) catabolic process
I0016829molecular_functionlyase activity
I0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
I1902777biological_process6-sulfoquinovose(1-) catabolic process
J0016829molecular_functionlyase activity
J0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
J1902777biological_process6-sulfoquinovose(1-) catabolic process
K0016829molecular_functionlyase activity
K0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
K1902777biological_process6-sulfoquinovose(1-) catabolic process
L0016829molecular_functionlyase activity
L0061595molecular_function6-deoxy-6-sulfofructose-1-phosphate aldolase activity
L1902777biological_process6-sulfoquinovose(1-) catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue SO4 A 301
ChainResidue
AGLN23
ALEU225
ASER226
ASER227
AALA251
AGLY252
AARG253
AHOH450
AHOH476

site_idAC2
Number of Residues9
Detailsbinding site for residue SO4 B 301
ChainResidue
BGLN23
BLEU225
BSER226
BSER227
BALA251
BGLY252
BARG253
BHOH415
BHOH422

site_idAC3
Number of Residues9
Detailsbinding site for residue SO4 C 301
ChainResidue
CGLN23
CLEU225
CSER226
CSER227
CALA251
CGLY252
CARG253
CHOH446
CHOH448

site_idAC4
Number of Residues9
Detailsbinding site for residue SO4 D 301
ChainResidue
DGLN23
DLEU225
DSER226
DSER227
DALA251
DGLY252
DARG253
DHOH443
DHOH468

site_idAC5
Number of Residues9
Detailsbinding site for residue SO4 E 301
ChainResidue
EGLN23
ELEU225
ESER226
ESER227
EALA251
EGLY252
EARG253
EHOH427
EHOH441

site_idAC6
Number of Residues7
Detailsbinding site for residue SO4 F 301
ChainResidue
FGLN23
FLEU225
FSER226
FSER227
FALA251
FGLY252
FARG253

site_idAC7
Number of Residues9
Detailsbinding site for residue SO4 G 301
ChainResidue
GGLN23
GLEU225
GSER226
GSER227
GALA251
GGLY252
GARG253
GHOH416
GHOH427

site_idAC8
Number of Residues9
Detailsbinding site for residue SO4 H 301
ChainResidue
HGLN23
HLEU225
HSER226
HSER227
HALA251
HGLY252
HARG253
HHOH413
HHOH425

site_idAC9
Number of Residues9
Detailsbinding site for residue SO4 I 301
ChainResidue
IGLN23
ILEU225
ISER226
ISER227
IALA251
IGLY252
IARG253
IHOH455
IHOH468

site_idAD1
Number of Residues9
Detailsbinding site for residue SO4 J 301
ChainResidue
JGLN23
JLEU225
JSER226
JSER227
JALA251
JGLY252
JARG253
JHOH429
JHOH465

site_idAD2
Number of Residues9
Detailsbinding site for residue SO4 K 301
ChainResidue
KGLN23
KLEU225
KSER226
KSER227
KALA251
KGLY252
KARG253
KHOH439
KHOH467

site_idAD3
Number of Residues9
Detailsbinding site for residue SO4 L 301
ChainResidue
LSER226
LSER227
LALA251
LGLY252
LARG253
LHOH440
LHOH499
LGLN23
LLEU225

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_01912, ECO:0000269|PubMed:33791429, ECO:0007744|PDB:7NE2
ChainResidueDetails
ALYS193
JLYS193
KLYS193
LLYS193
BLYS193
CLYS193
DLYS193
ELYS193
FLYS193
GLYS193
HLYS193
ILYS193

238268

PDB entries from 2025-07-02

PDB statisticsPDBj update infoContact PDBjnumon