Structure of PDB 1b57 Chain B Binding Site BS03

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 IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1b57 Chain B Residue 362 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)		H91 H129
Binding residue
(residue number reindexed from 1)		H91 H129
Annotation score1
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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Molecular Function
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Biological Process
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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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