Structure of PDB 2zyf Chain A

Receptor sequence

>2zyfA (length=314) Species: 262724 (Thermus thermophilus HB27)

MREWKIIDSTLREGEQFEKANFSTQDKVEIAKALDEFGIEYIEVTTPVAS
PQSRKDAEVLASLGLKAKVVTHIQCRLDAAKVAVETGVQGIDLLFGTSKG
RDIPRIIEEAKEVIAYIREAAPHVEVRFSAEDTFRSEEQDLLAVYEAVAP
YVDRVGLADTVGVATPRQVYALVREVRRVVGPRVDIEFHGHNDTGCAIAN
AYEAIEAGATHVDTTILGIGERNGITPLGGFLARMYTLQPEYVRRKYKLE
MLPELDRMVARMVGVEIPFNNYITGETAFSHKAGMHLKAIYINPEAYEPY
PPEVFGVKRKLIIA

3D structure

• PDB: 2zyf Mechanism of substrate recognition and insight into feedback inhibition of homocitrate synthase from thermus thermophilus
• Chain: A
• Resolution: 2.15 Å

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.

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	AKG	A	R12 H72 L94 R133 T166 H195	R12 H72 L94 R127 T160 H189
BS02	MG	A	E13 H195 H197	E13 H189 H191

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