Structure of PDB 3bzn Chain A

Receptor sequence
>3bznA (length=430) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MQSLTTALENLLRHLSQEIPATPGIRVIDIPFPLKDAFDALSWLASQQTY
PQFYWQQRNGDEEAVVLGAITRFTSLDQAQRFLRQHPEHADLRIWGLNAF
DPSQGNLLLPRLEWRRCGGKATLRLTLFSESSLQHDAIQAKEFIATLVSI
KPLPGLHLTTTREQHWPDKTGWTQLIELATKTIAEGELDKVVLARATDLH
FASPVNAAAMMAASRRLNLNCYHFYMAFDGENAFLGSSPERLWRRRDKAL
RTEALAGTVANNPDDKQAQQLGEWLMADDKNQRENMLVVEDICQRLQADT
QTLDVLPPQVLRLRKVQHLRRCIWTSLNKADDVICLHQLQPTAAVAGLPR
DLARQFIARHEPFTREWYAGSAGYLSLQQSEFCVSLRSAKISGNVVRLYA
GAGIVRGSDPEQEWQEIDNKAAGLRTLLQM
3D structure
PDB3bzn Structure of isochorismate synthase in complex with magnesium.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K190 E240 A256 E284 H318 A344 Y368 R387 G403 E416 K420
Catalytic site (residue number reindexed from 1) K190 E240 A256 E284 H318 A344 Y368 R387 G403 E416 K420
Enzyme Commision number 5.4.4.2: isochorismate synthase.
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 MG A E284 E416 E284 E416
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008909 isochorismate synthase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0009058 biosynthetic process
GO:0009234 menaquinone biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:3bzn, PDBe:3bzn, PDBj:3bzn
PDBsum3bzn
PubMed18453696
UniProtP38051|MENF_ECOLI Isochorismate synthase MenF (Gene Name=menF)

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