Structure of PDB 1i1k Chain A Binding Site BS01

Receptor Information
>1i1k Chain A (length=298) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYDSHKGPVVFRH
REHMQRLHDSAKIYRFPVSQSIDELMEACRDVIRKNNLTSAYIRPLIFVG
DVGMGVNPPAGYSTDVIIAAFPWALEQGIDAMVSSWNRAAPNTIPTAAKA
GGNYLSSLLVGSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTP
PFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLADEVFMSGTAAE
ITPVRSVDGIQVGEGRCGPVTKRIQQAFFGLFTGETEDKWGWLDQVNQ
Ligand information
Ligand IDPLP
InChIInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain1i1k Chain A Residue 413 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1i1k Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2-methylleucine: induced fit and substrate recognition of the enzyme.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		R59 K159 Y164 E193 G196 E197 L217 I220 T221 T257
Binding residue
(residue number reindexed from 1)		R56 K149 Y154 E183 G186 E187 L207 I210 T211 T247
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K159
Catalytic site (residue number reindexed from 1) K149
Enzyme Commision number 2.6.1.42: branched-chain-amino-acid transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004084 branched-chain-amino-acid transaminase activity
GO:0008483 transaminase activity
GO:0042802 identical protein binding
GO:0052654 L-leucine-2-oxoglutarate transaminase activity
GO:0052655 L-valine-2-oxoglutarate transaminase activity
GO:0052656 L-isoleucine-2-oxoglutarate transaminase activity
Biological Process
GO:0006532 aspartate biosynthetic process
GO:0008652 amino acid biosynthetic process
GO:0009081 branched-chain amino acid metabolic process
GO:0009082 branched-chain amino acid biosynthetic process
GO:0009097 isoleucine biosynthetic process
GO:0009098 L-leucine biosynthetic process
GO:0009099 L-valine biosynthetic process
GO:0046394 carboxylic acid biosynthetic 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:1i1k, PDBe:1i1k, PDBj:1i1k
PDBsum1i1k
PubMed11412098
UniProtP0AB80|ILVE_ECOLI Branched-chain-amino-acid aminotransferase (Gene Name=ilvE)

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