Structure of PDB 1kl7 Chain A

Receptor sequence
>1kl7A (length=509) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
PNASQVYRSTRSSSPKTISFEEAIIQGLATDGGLFIPPTIPQVDQATLFN
DWSKLSFQDLAFAIMRLYIAQEEIPDADLKDLIKRSYSTFRSDEVTPLVQ
NVTGDKENLHILELFHGPTYAFKDVALQFVGNLFEYFLQRTNANLPEGEK
KQITVVGATSGDTGSAAIYGLRGKKDVSVFILYPTGRISPIQEEQMTTVP
DENVQTLSVTGTFDNCQDIVKAIFGDKEFNHNVGAVNSINWARILAQMTY
YFYSFFQATNGKDSKKVKFVVPSGNFGDILAGYFAKKMGLPIEKLAIATN
ENDILDRFLKSGLYERSDKVAATLSPAMDILISSNFERLLWYLAREYLAN
GDDLKAGEIVNNWFQELKTNGKFQVDKSIIEGASKDFTSERVSNEETSET
IKKIYESSVNPKHYILDPHTAVGVCATERLIAKDNDKSIQYISLSTAHPA
KFADAVNNALSGFSNYSFEKDVLPEELKKLSTLKKKLKFIERADVELVKN
AIEEELAKM
3D structure
PDB1kl7 Structure and function of threonine synthase from yeast.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K124
Catalytic site (residue number reindexed from 1) K123
Enzyme Commision number 4.2.3.1: threonine 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 PLP A F123 K124 S276 G277 N278 D281 A330 H422 T449 F122 K123 S273 G274 N275 D278 A327 H419 T446
Gene Ontology
Molecular Function
GO:0004795 threonine synthase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009088 threonine biosynthetic process
Cellular Component
GO:0005634 nucleus
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:1kl7, PDBe:1kl7, PDBj:1kl7
PDBsum1kl7
PubMed11756443
UniProtP16120|THRC_YEAST Threonine synthase (Gene Name=THR4)

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