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Structure of PDB 1b57 Chain B Binding Site BS04

Receptor Information
>1b57 Chain B (length=346) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAA
KVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHY
GVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESL
QENIEICSKYLERMSKIGMTLEIELGCTGGEELYTQPEDVDYAYTELSKI
SPRFTIAASFGNVHGVYKPGNVVLTPTILRDSQEYVSKKHNLPHNSLNFV
FHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANEAYLQG
QLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL
Ligand information
Ligand IDPGH
InChIInChI=1S/C2H6NO6P/c4-2(3-5)1-9-10(6,7)8/h5H,1H2,(H,3,4)(H2,6,7,8)
InChIKeyBAXHHWZKQZIJID-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCC(=O)NO
OpenEye OEToolkits 1.5.0C(C(=O)NO)OP(=O)(O)O
CACTVS 3.341ONC(=O)CO[P](O)(O)=O
FormulaC2 H6 N O6 P
NamePHOSPHOGLYCOLOHYDROXAMIC ACID
ChEMBLCHEMBL371668
DrugBankDB03026
ZINC
PDB chain1b57 Chain B Residue 359 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1b57 The crystal structure of Escherichia coli class II fructose-1, 6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		D109 H110 H226 G227 H264 G265 S267 N286 I287 D288 T289
Binding residue
(residue number reindexed from 1)		D109 H110 H214 G215 H252 G253 S255 N274 I275 D276 T277
Annotation score2
Binding affinityPDBbind-CN: -logKd/Ki=8.00,Ki=0.01uM
Enzymatic activity
Catalytic site (original residue number in PDB) D109 H110 E182 H226 H264 N286
Catalytic site (residue number reindexed from 1) D109 H110 E182 H214 H252 N274
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
Gene Ontology
Molecular Function
GO:0004332 fructose-bisphosphate aldolase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0016832 aldehyde-lyase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1b57, PDBe:1b57, PDBj:1b57
PDBsum1b57
PubMed10080900
UniProtP0AB71|ALF_ECOLI Fructose-bisphosphate aldolase class 2 (Gene Name=fbaA)

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