Structure of PDB 6uxj Chain C

Receptor sequence
>6uxjC (length=472) Species: 3847 (Glycine max) [Search protein sequence]
SHMDPVSVWGNTPLATVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVI
EALGSALTNKYSEGMPGNRYYGGNEYIDQIENLCRSRALQAFHLDAQSWG
VNVQPYSGSPANFAAYTAVLNPHDRIMGLDLPSGGHLTHGYYTSGGKKIS
ATSIYFESLPYKVNSTTGYIDYDRLEEKALDFRPKLIICGGSAYPRDWDY
KRFREVADKCGALLLCDMAHTSGLVAAQEVNSPFEYCDIVTTTTHKSLRG
PRAGMIFYRKGPKPPKKGQPENAVYDFEDKINFAVFPSLQGGPHNHQIGA
LAVALKQAASPGFKAYAKQVKANAVALGKYLMGKGYSLVTGGTENHLVLW
DLRPLGLTGNKVEKLCDLCNITVNKNAVFGDSSALAPGGVRIGAPAMTSR
GLVEKDFEQIGEFLHRAVTLTLEIQKEHGKLLKDFNKGLVNNKAIEDLKA
DVEKFSALFDMPGFLVSEMKYK
3D structure
PDB6uxj Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode.
ChainC
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y59 E61 D215 T241 K244 R250
Catalytic site (residue number reindexed from 1) Y61 E63 D217 T243 K246 R252
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 PLG C S39 S105 G106 S107 H134 G189 S190 D215 A217 H218 H243 K244 R389 S41 S107 G108 S109 H136 G191 S192 D217 A219 H220 H245 K246 R391
BS02 FFO C L129 G132 G133 H134 L135 Y139 S190 N374 A382 L131 G134 G135 H136 L137 Y141 S192 N376 A384 MOAD: Kd=17uM
BS03 PLG C Y59 Y69 G289 Y61 Y71 G291
BS04 FFO C Y68 Y69 F281 Y70 Y71 F283 MOAD: Kd=17uM
Gene Ontology
Molecular Function
GO:0004372 glycine hydroxymethyltransferase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0019264 glycine biosynthetic process from serine
GO:0035999 tetrahydrofolate interconversion

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Molecular Function
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Biological Process
External links
PDB RCSB:6uxj, PDBe:6uxj, PDBj:6uxj
PDBsum6uxj
PubMed32014996
UniProtA0A0R0IK90

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