Structure of PDB 5eig Chain D Binding Site BS01

Receptor Information
>5eig Chain D (length=387) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGASGFTYSRS
GNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDV
YGGTNRYFRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPT
QKVIDIEGCAHIVHKHGDIILVVDNTFMSPYFQRPLALGADISMYSATKY
MNGHSDVVMGLVSVNCESLHNRLRFLQNSLGAVPSPIDCYLCNRGLKTLH
VRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQHELVKRQCTGCTGM
VTFYIKGTLQHAEIFLKNLKLFTLAVSLGGFESLAELPAIMTHASVLKND
RDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPP
Ligand information
Ligand IDCYS
InChIInChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
InChIKeyXUJNEKJLAYXESH-REOHCLBHSA-N
SMILES
SoftwareSMILES
CACTVS 3.341N[CH](CS)C(O)=O
OpenEye OEToolkits 1.5.0C([C@@H](C(=O)O)N)S
CACTVS 3.341N[C@@H](CS)C(O)=O
ACDLabs 10.04O=C(O)C(N)CS
OpenEye OEToolkits 1.5.0C(C(C(=O)O)N)S
FormulaC3 H7 N O2 S
NameCYSTEINE
ChEMBLCHEMBL863
DrugBankDB00151
ZINCZINC000000895042
PDB chain5eig Chain C Residue 501 [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]
PDB5eig Systemic Depletion of Serum L-Cyst(e)ine with an Engineered Human Enzyme Mediates Potent Induction of ROS and Cancer Ablation
Resolution2.7 Å
Binding residue
(original residue number in PDB)		R62 N241
Binding residue
(residue number reindexed from 1)		R49 N228
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) R62 Y114 D187 K212
Catalytic site (residue number reindexed from 1) R49 Y101 D174 K199
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5eig, PDBe:5eig, PDBj:5eig
PDBsum5eig
PubMed
UniProtP32929|CGL_HUMAN Cystathionine gamma-lyase (Gene Name=CTH)

[Back to BioLiP]