Structure of PDB 4f4f Chain B

Receptor sequence
>4f4fB (length=464) Species: 224914 (Brucella melitensis bv. 1 str. 16M) [Search protein sequence]
SMKYVSTRGEAPVLGFSDALLAGLARDGGLYLPQEYPQFTAEQIRALRGK
SYVEVALAVLTPFTGGEIPAADFERMVREAYGTFRHDAVCPLVQTDANEF
VLELFHGPTLAFKDVAMQLLARMMDYVLAQRGERATIVGATSGDTGGAAI
EAFGGRDNTDIFILFPNGRVSPVQQRQMTSSGFSNVHALSIEGNFDDCQN
LVKGMFNDLEFCDALSLSGVNSINWARIMPQVVYYFTAALSLGAPDRAVS
FTVPTGNFGDIFAGYVAKRMGLPIEQLIIATNDNDILSRTLESGAYEMRG
VAQTTSPSMDIQISSNFERLLFEAHGRDAAAVRGLMQGLKQSGGFTISEK
PLSAIRSEFSAGRSTVDETAATIESVLSKDGYLLDPHSAIGVKVAREKAS
GTAPMVVLATAHPAKFPDAVKAACGVEPQLPAWLCDLMQRKESFTVLHNE
LKIVEEYVRHHSRA
3D structure
PDB4f4f X-Ray crystal structure of PLP bound Threonine synthase from Brucella melitensis
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K112
Catalytic site (residue number reindexed from 1) K113
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 B F111 K112 T254 G255 N256 F257 D259 S307 M308 H386 T409 F112 K113 T255 G256 N257 F258 D260 S308 M309 H387 T410
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4f4f, PDBe:4f4f, PDBj:4f4f
PDBsum4f4f
PubMed
UniProtQ8YFS0

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