Structure of PDB 1kkj Chain A

Receptor sequence
>1kkjA (length=405) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
MKYLPQQDPQVFAAIEQERKRQHAKIELIASENFVSRAVMEAQGSVLTNK
YAEGYPGRRYYGGCEYVDIVEELARERAKQLFGAEHANVQPHSGAQANMA
VYFTVLEHGDTVLGMNLSHGGHLTHGSPVNFSGVQYNFVAYGVDPETHVI
DYDDVREKARLHRPKLIVAAASAYPRIIDFAKFREIADEVGAYLMVDMAH
IAGLVAAGLHPNPVPYAHFVTTTTHKTLRGPRGGMILCQEQFAKQIDKAI
FPGIQGGPLMHVIAAKAVAFGEALQDDFKAYAKRVVDNAKRLASALQNEG
FTLVSGGTDNHLLLVDLRPQQLTGKTAEKVLDEVGITVNKNTIPYDPESP
FVTSGIRIGTAAVTTRGFGLEEMDEIAAIIGLVLKNVGSEQALEEARQRV
AALTD
3D structure
PDB1kkj Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: insights into the catalytic mechanism.
ChainA
Resolution1.93 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y51 E53 D197 T223 K226 R232
Catalytic site (residue number reindexed from 1) Y51 E53 D197 T223 K226 R232
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 PLP A S93 G94 A95 H122 S172 D197 A199 H200 T223 H225 K226 S93 G94 A95 H122 S172 D197 A199 H200 T223 H225 K226
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:1kkj, PDBe:1kkj, PDBj:1kkj
PDBsum1kkj
PubMed11877399
UniProtQ7SIB6

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