Structure of PDB 4n0w Chain A

Receptor sequence
>4n0wA (length=416) Species: 216591 (Burkholderia cenocepacia J2315) [Search protein sequence]
SMFDRAQSTIANVDPEIFAAIEQENRRQEDHIELIASENYTSPAVMAAQG
SQLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRVKQLFGAEAANVQPNSG
SQANQGVFFAMLKPGDTIMGMSLAHGGHLTHGSPVNMSGKWFNVVSYGLN
ENEDIDYDAAEKLANEHKPKLIVAGASAFALKIDFERLAKIAKSVGAYLM
VDMAHYAGLIAAGVYPNPVPHADFVTTTTHKSLRGPRGGVILMKAEYEKP
INSAIFPGIQGGPLMHVIAAKAVAFKEALSPEFKEYQQKVVENARVLAET
LVKRGLRIVSGRTESHVMLVDLRAKHITGKAAEAALGAAHITVNKNAIPN
DPEKPFVTSGIRLGSPAMTTRGFGPAEAEQVGNLIADVLENPEDAATIER
VRAQVAELTKRFPVYR
3D structure
PDB4n0w X-ray crystal structure of a serine hydroxymethyltransferase from Burkholderia cenocepacia with covalently attached pyridoxal phosphate
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y56 E58 D201 T227 K230 R236
Catalytic site (residue number reindexed from 1) Y57 E59 D202 T228 K231 R237
Enzyme Commision number 2.1.2.1: glycine hydroxymethyltransferase.
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 A S98 G99 S100 H127 D201 A203 H204 K230 S99 G100 S101 H128 D202 A204 H205 K231
Gene Ontology
Molecular Function
GO:0004372 glycine hydroxymethyltransferase activity
GO:0008270 zinc ion binding
GO:0016740 transferase activity
GO:0030170 pyridoxal phosphate binding
GO:0050897 cobalt ion binding
GO:0070905 serine binding
Biological Process
GO:0006545 glycine biosynthetic process
GO:0006565 L-serine catabolic process
GO:0006730 one-carbon metabolic process
GO:0008652 amino acid biosynthetic process
GO:0019264 glycine biosynthetic process from serine
GO:0035999 tetrahydrofolate interconversion
GO:0046653 tetrahydrofolate metabolic process
GO:0046655 folic acid metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:4n0w, PDBe:4n0w, PDBj:4n0w
PDBsum4n0w
PubMed
UniProtB4ECY9

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