Structure of PDB 1yjy Chain A Binding Site BS02

Receptor Information
>1yjy Chain A (length=405) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKYLPQQDPQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNK
YAEGYPGRRYYGGCEYVDIVEELARERAKQLFGAEHANVQPHSGAQANMA
VYFTVLEHGDTVLGMNLSHGGHLTHGSPVNFSGVQYNFVAYGVDPETHVI
DYDDVREKARLHRPKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAH
IAGLVAAGLHPNPVPYAHFVTTTTHMTLRGPRGGMILCQEQFAKQIDKAI
FPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLASALQNEG
FTLVSGGTDNHLLLVDLRPQQLTGKTAEKVLDEVGITVNKNTIPYDPESP
FVTSGIRIGTAAVTTRGFGLEEMDEIAAIIGLVLKNVGSEQALEEARQRV
AALTD
Ligand information
Ligand IDSER
InChIInChI=1S/C3H7NO3/c4-2(1-5)3(6)7/h2,5H,1,4H2,(H,6,7)/t2-/m0/s1
InChIKeyMTCFGRXMJLQNBG-REOHCLBHSA-N
SMILES
SoftwareSMILES
CACTVS 3.341N[CH](CO)C(O)=O
OpenEye OEToolkits 1.5.0C(C(C(=O)O)N)O
CACTVS 3.341N[C@@H](CO)C(O)=O
ACDLabs 10.04O=C(O)C(N)CO
OpenEye OEToolkits 1.5.0C([C@@H](C(=O)O)N)O
FormulaC3 H7 N O3
NameSERINE
ChEMBLCHEMBL11298
DrugBankDB00133
ZINCZINC000000895034
PDB chain1yjy Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1yjy Role of Lys-226 in the Catalytic Mechanism of Bacillus Stearothermophilus Serine Hydroxymethyltransferase-Crystal Structure and Kinetic Studies
Resolution2.25 Å
Binding residue
(original residue number in PDB)		S31 H122 H200 R357
Binding residue
(residue number reindexed from 1)		S31 H122 H200 R357
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) Y51 E53 D197 T223 M226 R232
Catalytic site (residue number reindexed from 1) Y51 E53 D197 T223 M226 R232
Enzyme Commision number 2.1.2.1: glycine hydroxymethyltransferase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
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:1yjy, PDBe:1yjy, PDBj:1yjy
PDBsum1yjy
PubMed15865438
UniProtQ7SIB6

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