Structure of PDB 1lw5 Chain D Binding Site BS01

Receptor Information
>1lw5 Chain D (length=344) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MMIDLRSDTVTKPTEEMRKAMAQAEVGDDVYGEDPTINELERLAAETFGK
EAALFVPSGTMGNQVSIMAHTQRGDEVILEADSHIFWYEVGAMAVLSGVM
PHPVPGKNGAMDPDDVRKAIRPRNIHFPRTSLIAIENTHNRSGGRVVPLE
NIKEICTIAKEHGINVHIDGARIFNASIASGVPVKEYAGYADSVMFCLSK
GLCAPVGSVVVGDRDFIERARKARKMLGGGMRQAGVLAAAGIIALTKMVD
RLKEDHENARFLALKLKEIGYSVNPEDVKTNMVILRTDNLKVNAHGFIEA
LRNSGVLANAVSDTEIRLVTHKDVSRNDIEEALNIFEKLFRKFS
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1lw5 Chain A Residue 1006 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1lw5 X-ray Structures of Threonine Aldolase Complexes: Structural Basis of Substrate Recognition
Resolution2.05 Å
Binding residue
(original residue number in PDB)
T8 T10 S198 A203
Binding residue
(residue number reindexed from 1)
T9 T11 S199 A204
Annotation score1
Enzymatic activity
Enzyme Commision number 4.1.2.5: L-threonine aldolase.
Gene Ontology
Molecular Function
GO:0008732 L-allo-threonine aldolase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0006545 glycine biosynthetic process
GO:0006567 threonine catabolic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1lw5, PDBe:1lw5, PDBj:1lw5
PDBsum1lw5
PubMed12269813
UniProtQ9X266

[Back to BioLiP]