Structure of PDB 4bhd Chain B Binding Site BS01

Receptor Information
>4bhd Chain B (length=395) Species: 2190 (Methanocaldococcus jannaschii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MYSDVPKFIRDVSIKQHEWMRESIKLIASENITSLAVREACATDFMGCKY
IDEVETLCIELSKELFKAEHANVQPTSGVVANLAVFFAETMALSVPDGGH
ISHWNHPFDPEEMNIDADAMVKKILEEKPKLILFGGSLFPFPHPVADAYE
AAQEVGAKIAYDGAHVLGLIAGKQFQDPLREGAEYLMGSTHKTFFGPQGG
VILTTKENADKIDSHVFPGVVSNHHLHHKAGLAIALAEMLEFGEAYAKQV
IKNAKALAQALYERGFNVLCEHKDFTESHQVIIDIESSPDIEFSASELAK
MYEEANIILNKNLLPWDDVNNSDNPSGIRLGTQECTRLGMKEKEMEEIAE
FMKRIAIDKEKPEKVREDVKEFAKEYSTIHYSFDEGDGFKYLRFY
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain4bhd Chain B Residue 1430 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4bhd The Crystal Structure of Archaeal Serine Hydroxymethyltransferase Reveals Idiosyncratic Features Likely Required to Withstand High Temperatures.
Resolution2.83 Å
Binding residue
(original residue number in PDB)		S30 S171 H199 R363
Binding residue
(residue number reindexed from 1)		S29 S137 H165 R329
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D196 S223 K226 Q232
Catalytic site (residue number reindexed from 1) D162 S189 K192 Q198
Enzyme Commision number 2.1.2.-
4.1.2.49: L-allo-threonine aldolase.
Gene Ontology
Molecular Function
GO:0004372 glycine hydroxymethyltransferase activity
GO:0008732 L-allo-threonine aldolase activity
GO:0016740 transferase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006545 glycine biosynthetic 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
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4bhd, PDBe:4bhd, PDBj:4bhd
PDBsum4bhd
PubMed25257552
UniProtQ58992|GLYA_METJA Serine hydroxymethyltransferase (Gene Name=glyA)

[Back to BioLiP]