Structure of PDB 4l27 Chain A

Receptor sequence
>4l27A (length=485) Species: 9606 (Homo sapiens) [Search protein sequence]
PLWIRPDAPSRCTWQLGRSESPHHHTAPAKSPKILPDILKKIGDTPMVRI
NKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI
IEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTP
TNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQ
QCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEE
LNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQE
GLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWML
QKGFLKEEEKKPWWWHLRVQELGLSAPLTVLITCGTIEILREKGFNQAPV
VDEILGMVTLGNMLSSLLAGKVQPSDVGKVIYKQFKQIRLTDTLGRLSHI
LEMDHFALVVHERQMVFGVVTAIDLLNFVAAQERD
3D structure
PDB4l27 Structural basis of regulation and oligomerization of human cystathionine beta-synthase, the central enzyme of transsulfuration.
ChainA
Resolution3.391 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 D239 S243 L245 S307 P333
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 PLP A K119 N149 V255 G256 T257 G258 T260 G305 I306 S349 P375 D376 K77 N107 V213 G214 T215 G216 T218 G263 I264 S307 P333 D334
BS02 HEM A S50 R51 C52 T53 W54 S63 P64 H65 A226 P229 Y233 R266 T313 S10 R11 C12 T13 W14 S21 P22 H23 A184 P187 Y191 R224 T271
Gene Ontology
Molecular Function
GO:0004122 cystathionine beta-synthase activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0019825 oxygen binding
GO:0019899 enzyme binding
GO:0020037 heme binding
GO:0030170 pyridoxal phosphate binding
GO:0031625 ubiquitin protein ligase binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0050421 nitrite reductase (NO-forming) activity
GO:0070025 carbon monoxide binding
GO:0070026 nitric oxide binding
GO:0072341 modified amino acid binding
GO:1904047 S-adenosyl-L-methionine binding
Biological Process
GO:0001958 endochondral ossification
GO:0001974 blood vessel remodeling
GO:0006534 cysteine metabolic process
GO:0006535 cysteine biosynthetic process from serine
GO:0006563 L-serine metabolic process
GO:0006565 L-serine catabolic process
GO:0006801 superoxide metabolic process
GO:0009069 serine family amino acid metabolic process
GO:0010749 regulation of nitric oxide mediated signal transduction
GO:0019343 cysteine biosynthetic process via cystathionine
GO:0019344 cysteine biosynthetic process
GO:0019346 transsulfuration
GO:0019448 L-cysteine catabolic process
GO:0021587 cerebellum morphogenesis
GO:0031667 response to nutrient levels
GO:0042262 DNA protection
GO:0043066 negative regulation of apoptotic process
GO:0043418 homocysteine catabolic process
GO:0044272 sulfur compound biosynthetic process
GO:0050667 homocysteine metabolic process
GO:0051593 response to folic acid
GO:0060135 maternal process involved in female pregnancy
GO:0060351 cartilage development involved in endochondral bone morphogenesis
GO:0070814 hydrogen sulfide biosynthetic process
GO:0071456 cellular response to hypoxia
GO:0097746 blood vessel diameter maintenance
Cellular Component
GO:0005634 nucleus
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:4l27, PDBe:4l27, PDBj:4l27
PDBsum4l27
PubMed24043838
UniProtP35520|CBS_HUMAN Cystathionine beta-synthase (Gene Name=CBS)

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