Structure of PDB 6uxj Chain D

Receptor sequence
>6uxjD (length=472) Species: 3847 (Glycine max) [Search protein sequence]
HMDPVSVWGNTPLATVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIE
ALGSALTNKYSEGMPGNRYYGGNEYIDQIENLCRSRALQAFHLDAQSWGV
NVQPYSGSPANFAAYTAVLNPHDRIMGLDLPSGGHLTHGYYTSGGKKISA
TSIYFESLPYKVNSTTGYIDYDRLEEKALDFRPKLIICGGSAYPRDWDYK
RFREVADKCGALLLCDMAHTSGLVAAQEVNSPFEYCDIVTTTTHKSLRGP
RAGMIFYRKGPKPPKKGQPENAVYDFEDKINFAVFPSLQGGPHNHQIGAL
AVALKQAASPGFKAYAKQVKANAVALGKYLMGKGYSLVTGGTENHLVLWD
LRPLGLTGNKVEKLCDLCNITVNKNAVFGDSSALAPGGVRIGAPAMTSRG
LVEKDFEQIGEFLHRAVTLTLEIQKEHGKLLKDFNKGLVNNKAIEDLKAD
VEKFSALFDMPGFLVSEMKYKD
3D structure
PDB6uxj Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode.
ChainD
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) Y60 E62 D216 T242 K245 R251
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 D Y59 Y69 G289 Y60 Y70 G290
BS02 FFO D Y68 Y69 F281 Y69 Y70 F282 MOAD: Kd=17uM
BS03 PLG D S39 S105 G106 S107 H134 G189 S190 D215 A217 H218 H243 K244 R389 S40 S106 G107 S108 H135 G190 S191 D216 A218 H219 H244 K245 R390
BS04 FFO D L129 G132 G133 H134 L135 Y139 S190 N374 A382 L130 G133 G134 H135 L136 Y140 S191 N375 A383 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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