Structure of PDB 1czc Chain A

Receptor sequence
>1czcA (length=396) Species: 562 (Escherichia coli) [Search protein sequence]
MFENITTAPADPILGLADLLRADERPGKIDLGMGVYNDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGTGALRVAADFLAKNTSVRRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGTCTLVAADSETVDRAFSQMKAAIRVNYSSPPAHGASVVATILGN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFTIKQNGMFFF
GGLTKEQVLRLREEFGVYAVASGRLNVAGMTPDNLAPLCEAIVAVL
3D structure
PDB1czc Cocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: structural comparison with the enzyme-C4-dicarboxylic analog complex.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 PLP A G107 G108 T109 W140 D222 A224 S255 S257 K258 R266 G102 G103 T104 W130 D211 A213 S243 S245 K246 R254
BS02 GUA A I17 W140 N194 R386 I13 W130 N183 R374 MOAD: Kd=1.5mM
PDBbind-CN: -logKd/Ki=2.82,Kd=1.5mM
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:1czc, PDBe:1czc, PDBj:1czc
PDBsum1czc
PubMed10731702
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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