Structure of PDB 2ztj Chain A Binding Site BS02

Receptor Information

>2ztj Chain A (length=312) Species: 262724 (Thermus thermophilus HB27)

MREWKIIDSTLREGEQFEKANFSTQDKVEIAKALDEFGIEYIEVTTPVAS
PQSRKDAEVLASLGLKAKVVTHIQCRLDAAKVAVETGVQGIDLLFGTGRD
IPRIIEEAKEVIAYIREAAPHVEVRFSAEDTFRSEEQDLLAVYEAVAPYV
DRVGLADTVGVATPRQVYALVREVRRVVGPRVDIEFHGHNDTGCAIANAY
EAIEAGATHVDTTILGIGERNGITPLGGFLARMYTLQPEYVRRKYKLEML
PELDRMVARMVGVEIPFNNYITGETAFSHKAGMHLKAIYINPEAYEPYPP
EVFGVKRKLIIA

Ligand information

• Ligand ID: CU
• InChI: InChI=1S/Cu/q+2
• InChIKey: JPVYNHNXODAKFH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cu+2]
  CACTVS 3.341: [Cu++]
• Formula: Cu
• Name: COPPER (II) ION
• DrugBank: DB14552
• PDB chain: 2ztj Chain A Residue 384

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2ztj Mechanism of substrate recognition and insight into feedback inhibition of homocitrate synthase from Thermus thermophilus
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): E13 H195 H197
• Binding residue (residue number reindexed from 1): E13 H187 H189
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): Q16
• Catalytic site (residue number reindexed from 1): Q16
• Enzyme Commision number: 2.3.3.14: homocitrate synthase.

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004410 homocitrate synthase activity
• GO:0016740 transferase activity
• GO:0036440 citrate synthase activity
• GO:0046872 metal ion binding
• GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer

Biological Process

• GO:0009085 lysine biosynthetic process
• GO:0019752 carboxylic acid metabolic process
• GO:0019878 lysine biosynthetic process via aminoadipic acid
• GO:0043436 oxoacid metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2ztj, PDBe:2ztj, PDBj:2ztj
• PDBsum: 2ztj
• PubMed: 19996101
• UniProt: O87198|HOSA_THET2 Homocitrate synthase (Gene Name=lys20)