Structure of PDB 1jbq Chain D

Receptor sequence
>1jbqD (length=348) Species: 9606 (Homo sapiens) [Search protein sequence]
WIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILKKIGDTPMVRI
NKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI
IEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTP
TESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLD
MLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQT
TYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGS
AGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFL
3D structure
PDB1jbq Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein.
ChainD
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K119 S147 D281 S285 L287 S349 P375
Catalytic site (residue number reindexed from 1) K77 S105 D232 S236 L238 S300 P326
Enzyme Commision number 4.2.1.22: cystathionine beta-synthase.
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 HEM D R51 C52 T53 W54 R58 E62 S63 P64 H65 R224 A226 P229 L230 Y233 R266 R9 C10 T11 W12 R16 E20 S21 P22 H23 R175 A177 P180 L181 Y184 R217
BS02 PLP D K119 N149 V255 G256 T257 G258 G259 T260 G305 S349 P375 D376 K77 N107 V206 G207 T208 G209 G210 T211 G256 S300 P326 D327
Gene Ontology
Molecular Function
GO:0004122 cystathionine beta-synthase activity
Biological Process
GO:0006535 cysteine biosynthetic process from serine
GO:0019343 cysteine biosynthetic process via cystathionine
Cellular Component
GO:0005737 cytoplasm

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Biological Process
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Cellular Component
External links
PDB RCSB:1jbq, PDBe:1jbq, PDBj:1jbq
PDBsum1jbq
PubMed11483494
UniProtP35520|CBS_HUMAN Cystathionine beta-synthase (Gene Name=CBS)

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