Structure of PDB 5tsu Chain A Binding Site BS01

Receptor Information
>5tsu Chain A (length=384) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGGFNYSRSGN
PTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYG
GTNLYFRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQK
VIDIEGCAHIVHKHGDIILVVDNTFMSPYFQRPLALGADISMYSATKYMN
GHSDVVMGLVSVNCESLHNRLRFLQNSLGAVPSPIDCYLCNRGLKTLHVR
MEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQHELVKRQCTGCTGMVT
FYIKGTLQHAEIFLKNLKLFTLAVSLGGFESLAELPAIMTHASVKNDRDV
LGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPP
Ligand information
Ligand IDMET
InChIInChI=1S/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1
InChIKeyFFEARJCKVFRZRR-BYPYZUCNSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CSCC[CH](N)C(O)=O
OpenEye OEToolkits 1.5.0CSCCC(C(=O)O)N
CACTVS 3.341CSCC[C@H](N)C(O)=O
OpenEye OEToolkits 1.5.0CSCC[C@@H](C(=O)O)N
ACDLabs 10.04O=C(O)C(N)CCSC
FormulaC5 H11 N O2 S
NameMETHIONINE
ChEMBLCHEMBL42336
DrugBankDB00134
ZINCZINC000001532529
PDB chain5tsu Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5tsu Structural Snapshots of an Engineered Cystathionine-gamma-lyase Reveal the Critical Role of Electrostatic Interactions in the Active Site.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		Y114 X212 S340 R375
Binding residue
(residue number reindexed from 1)		Y99 X197 S325 R359
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) R62 Y114 D187 K212
Catalytic site (residue number reindexed from 1) R47 Y99 D172 K197
Enzyme Commision number 4.4.1.1: cystathionine gamma-lyase.
4.4.1.2: homocysteine desulfhydrase.
Gene Ontology
Molecular Function
GO:0004123 cystathionine gamma-lyase activity
GO:0005515 protein binding
GO:0005516 calmodulin binding
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0044540 L-cystine L-cysteine-lyase (deaminating)
GO:0047982 homocysteine desulfhydrase activity
GO:0080146 L-cysteine desulfhydrase activity
GO:0098606 selenocystathionine gamma-lyase activity
Biological Process
GO:0006534 cysteine metabolic process
GO:0006629 lipid metabolic process
GO:0018272 protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine
GO:0019343 cysteine biosynthetic process via cystathionine
GO:0019344 cysteine biosynthetic process
GO:0019346 transsulfuration
GO:0030968 endoplasmic reticulum unfolded protein response
GO:0043066 negative regulation of apoptotic process
GO:0043123 positive regulation of canonical NF-kappaB signal transduction
GO:0044524 protein sulfhydration
GO:0051092 positive regulation of NF-kappaB transcription factor activity
GO:0051289 protein homotetramerization
GO:0070814 hydrogen sulfide biosynthetic process
GO:1904831 positive regulation of aortic smooth muscle cell differentiation
GO:1990830 cellular response to leukemia inhibitory factor
GO:2001234 negative regulation of apoptotic signaling pathway
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5tsu, PDBe:5tsu, PDBj:5tsu
PDBsum5tsu
PubMed28106980
UniProtP32929|CGL_HUMAN Cystathionine gamma-lyase (Gene Name=CTH)

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