Structure of PDB 1x29 Chain B Binding Site BS02

Receptor Information
>1x29 Chain B (length=396) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
Ligand information
Ligand IDPMG
InChIInChI=1S/C14H21N2O9P/c1-8-12(19)10(9(5-15-8)7-25-26(22,23)24)6-16-14(2,13(20)21)4-3-11(17)18/h5,16,19H,3-4,6-7H2,1-2H3,(H,17,18)(H,20,21)(H2,22,23,24)/t14-/m0/s1
InChIKeyCNIVMJHNGQZEAY-AWEZNQCLSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN[C@@](C)(CCC(O)=O)C(O)=O)c1O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN[C](C)(CCC(O)=O)C(O)=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@](C)(CCC(=O)O)C(=O)O)O
ACDLabs 10.04O=C(O)C(NCc1c(cnc(c1O)C)COP(=O)(O)O)(C)CCC(=O)O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNC(C)(CCC(=O)O)C(=O)O)O
FormulaC14 H21 N2 O9 P
NameN-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-2-METHYL-L-GLUTAMIC ACID;
N-PYRIDOXYL-2-METHYL-L-GLUTAMIC ACID-5'-MONOPHOSPHATE
ChEMBL
DrugBankDB04765
ZINCZINC000012504501
PDB chain1x29 Chain B Residue 1413 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1x29 Binding of C5-dicarboxylic substrate to aspartate aminotransferase: implications for the conformational change at the transaldimination step.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		I17 I37 G38 G107 G108 T109 W140 N194 D222 Y225 S255 S257 K258 R266 R386
Binding residue
(residue number reindexed from 1)		I13 I33 G34 G102 G103 T104 W130 N183 D211 Y214 S243 S245 K246 R254 R374
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W140 D222 A224 K258
Catalytic site (residue number reindexed from 1) W130 D211 A213 K246
Enzyme Commision number 2.6.1.1: aspartate transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0004838 L-tyrosine-2-oxoglutarate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
GO:0009094 L-phenylalanine biosynthetic process
GO:0033585 L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
Cellular Component
GO:0005737 cytoplasm
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:1x29, PDBe:1x29, PDBj:1x29
PDBsum1x29
PubMed15938611
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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