Structure of PDB 1lw5 Chain D

Receptor sequence
>1lw5D (length=344) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MMIDLRSDTVTKPTEEMRKAMAQAEVGDDVYGEDPTINELERLAAETFGK
EAALFVPSGTMGNQVSIMAHTQRGDEVILEADSHIFWYEVGAMAVLSGVM
PHPVPGKNGAMDPDDVRKAIRPRNIHFPRTSLIAIENTHNRSGGRVVPLE
NIKEICTIAKEHGINVHIDGARIFNASIASGVPVKEYAGYADSVMFCLSK
GLCAPVGSVVVGDRDFIERARKARKMLGGGMRQAGVLAAAGIIALTKMVD
RLKEDHENARFLALKLKEIGYSVNPEDVKTNMVILRTDNLKVNAHGFIEA
LRNSGVLANAVSDTEIRLVTHKDVSRNDIEEALNIFEKLFRKFS
3D structure
PDB1lw5 X-ray Structures of Threonine Aldolase Complexes: Structural Basis of Substrate Recognition
ChainD
Resolution2.05 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 4.1.2.5: L-threonine aldolase.
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 CA D T8 T10 S198 A203 T9 T11 S199 A204
BS02 CA D N326 E329 N327 E330
BS03 PLG D S6 G58 T59 H83 E135 D168 A170 R171 X199 R316 S7 G59 T60 H84 E136 D169 A171 R172 X200 R317
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]