Structure of PDB 1ve5 Chain D

Receptor sequence
>1ve5D (length=280) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
PSLQDLYAAFRRIAPYTHRTPLLTSRLLDGLLGKRLLLKAEHLQKTGSFK
ARGALSKALALENPKGLLAVSSGNHAQGVAYAAQVLGVKALVVMPVARAL
QEETGYALIHPFDDPLVIAGQGTAGLELLAQAGRMGVFPGAVLAPVGGGG
LLAGLATAVKALSPTTLVLGVEPEAADDAKRSLEAGRILRLEAPPRTRAD
GVRTLSLGERTFPILRERVDGILTVSEEALLEAERLLFTRTKQVVEPTGA
LPLAAVLEHGARLPQTLALLLSGGNRDFSP
3D structure
PDB1ve5 Crystal Structure of T.th. HB8 Threonine deaminase
ChainD
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K51 S57 S73 E203 A207 D209 G232 L302 S303
Catalytic site (residue number reindexed from 1) K50 S56 S72 E172 A176 D178 G201 L271 S272
Enzyme Commision number 4.3.1.19: threonine ammonia-lyase.
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 E203 A207 D209 E172 A176 D178
BS02 PLP D F50 K51 N75 G178 G179 G180 G181 V233 E277 T279 S303 G304 F49 K50 N74 G147 G148 G149 G150 V202 E246 T248 S272 G273
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0003941 L-serine ammonia-lyase activity
GO:0005524 ATP binding
GO:0018114 threonine racemase activity
GO:0030170 pyridoxal phosphate binding
GO:0030378 serine racemase activity
GO:0046872 metal ion binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0070179 D-serine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1ve5, PDBe:1ve5, PDBj:1ve5
PDBsum1ve5
PubMed
UniProtQ5SLL4

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