Structure of PDB 1xag Chain A

Receptor sequence
>1xagA (length=353) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
MKLQTTYPSNNYPIYVEHGAIKYIGTYLNQFDQSFLLIDEYVNQYFANKF
DDILSYENVHKVIIPAGEKTKTFEQYQETLEYILSHHVTRNTAIIAVGGG
ATGDFAGFVAATLLRGVHFIQVPTTILAHDSSVGGKVGINSKQGKNLIGA
FYRPTAVIYDLDFLKTLPFKQILSGYAEVYKHALLNGESATQDIEQHFKD
REILQSLNGMDKYIAKGIETKLDIVVADEKEQGVRKFLNLGHTFGHAVEY
YHKIPHGHAVMVGIIYQFIVANALFDSKHDISHYIQYLIQLGYPLDMITD
LDFETLYQYMLSDKKNDKQGVQMVLMRQFGDIVVQHVDQLTLQHACEQLK
TYF
3D structure
PDB1xag Comparison of ligand induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases.
ChainA
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R115 K136 E178 K221 E231 R235 N239 H242 H246 H256
Catalytic site (residue number reindexed from 1) R115 K136 E178 K221 E231 R235 N239 H242 H246 H256
Enzyme Commision number 4.2.3.4: 3-dehydroquinate synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003856 3-dehydroquinate synthase activity
GO:0016829 lyase activity
GO:0016838 carbon-oxygen lyase activity, acting on phosphates
GO:0046872 metal ion binding
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0009423 chorismate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1xag, PDBe:1xag, PDBj:1xag
PDBsum1xag
PubMed15465043
UniProtQ6GGU4|AROB_STAAR 3-dehydroquinate synthase (Gene Name=aroB)

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