Structure of PDB 8sui Chain B

Receptor sequence
>8suiB (length=402) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
KRDEALFELIALEEKRQREGLELIASENFVSKQVREAVGSVLTNKYAEGY
PGARYYGGCEVIDRVESLAIERAKALFGAAWANVQPHSGSQANMAVYMAL
MEPGDTLMGMDLAAGGHLTHGSRVNFSGKLYKVVSYGVRPDTELIDLEEV
RRLALEHRPKVIVAGASAYPRFWDFKAFREIADEVGAYLVVDMAHFAGLV
AAGLHPNPLPYAHVVTSTTHKTLRGPRGGLILSNDPELGKRIDKLIFPGI
QGGPLEHVIAGKAVAFFEALQPEFKEYSRLVVENAKRLAEELARRGYRIV
TGGTDNHLFLVDLRPKGLTGKEAEERLDAVGITVNKNAIPFDPKPPRVTS
GIRIGTPAITTRGFTPEEMPLVAELIDRALLEGPSEALREEVRRLALAHP
MP
3D structure
PDB8sui Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography.
ChainB
Resolution2.0 Å
3D
structure
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Enzymatic activity
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 SER B Y1060 Y1061 Y55 Y56
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8sui, PDBe:8sui, PDBj:8sui
PDBsum8sui
PubMed37532884
UniProtQ5SI56|GLYA_THET8 Serine hydroxymethyltransferase (Gene Name=glyA)

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