Structure of PDB 1lw5 Chain B

Receptor sequence
>1lw5B (length=343) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MIDLRSDTVTKPTEEMRKAMAQAEVGDDVYGEDPTINELERLAAETFGKE
AALFVPSGTMGNQVSIMAHTQRGDEVILEADSHIFWYEVGAMAVLSGVMP
HPVPGKNGAMDPDDVRKAIRPRNIHFPRTSLIAIENTHNRSGGRVVPLEN
IKEICTIAKEHGINVHIDGARIFNASIASGVPVKEYAGYADSVMFCLSKG
LCAPVGSVVVGDRDFIERARKARKMLGGGMRQAGVLAAAGIIALTKMVDR
LKEDHENARFLALKLKEIGYSVNPEDVKTNMVILRTDNLKVNAHGFIEAL
RNSGVLANAVSDTEIRLVTHKDVSRNDIEEALNIFEKLFRKFS
3D structure
PDB1lw5 X-ray Structures of Threonine Aldolase Complexes: Structural Basis of Substrate Recognition
ChainB
Resolution2.05 Å
3D
structure
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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 B N326 E329 N326 E329
BS02 PLG B S6 G58 T59 H83 E135 D168 A170 R171 X199 R316 S6 G58 T59 H83 E135 D168 A170 R171 X199 R316
BS03 PLP B G58 T59 H83 E135 D168 A170 R171 X199 G58 T59 H83 E135 D168 A170 R171 X199
BS04 CA B T8 T10 S198 A203 T8 T10 S198 A203
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:1lw5, PDBe:1lw5, PDBj:1lw5
PDBsum1lw5
PubMed12269813
UniProtQ9X266

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