Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T12241 | Target Info | |||
| Target Name | Cystathionine gamma-lyase (CTH) | ||||
| Synonyms | Gamma-cystathionase; Cysteine-protein sulfhydrase | ||||
| Target Type | Patented-recorded Target | ||||
| Gene Name | CTH | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Pyridoxal phosphate | Ligand Info | |||||
| Structure Description | Crystal structure of human cystathionase (Cystathionine gamma lyase) in complex with DL-propargylglycine | PDB:3COG | ||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] |
| PDB Sequence |
GFLPHFQHFA
19 TQAIHVGQDP29 EQWTSRAVVP39 PISLSTTFKQ49 GNPTRNCLEK73 AVAALDGAKY 83 CLAFASGLAA93 TVTITHLLKA103 GDQIICMDDV113 YGGTNRYFRQ123 VASEFGLKIS 133 FVDCSKIKLL143 EAAITPETKL153 VWIETPTNPT163 QKVIDIEGCA173 HIVHKHGDII 183 LVVDNTFMSP193 YFQRPLALGA203 DISMYSATKY213 MNGHSDVVMG223 LVSVNCESLH 233 NRLRFLQNSL243 GAVPSPIDCY253 LCNRGLKTLH263 VRMEKHFKNG273 MAVAQFLESN 283 PWVEKVIYPG293 LPSHPQHELV303 KRQCTGCTGM313 VTFYIKGTLQ323 HAEIFLKNLK 333 LFTLAESLGG343 FESLAELPAI353 MTHASVLKND363 RDVLGISDTL373 IRLSVGLEDE 383 EDLLEDLDQA393 LKAAHP
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: s-allylglycine | Ligand Info | |||||
| Structure Description | Crystal structure of human cystathionase (Cystathionine gamma lyase) in complex with DL-propargylglycine | PDB:3COG | ||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [1] |
| PDB Sequence |
GFLPHFQHFA
19 TQAIHVGQDP29 EQWTSRAVVP39 PISLSTTFKQ49 GNPTRNCLEK73 AVAALDGAKY 83 CLAFASGLAA93 TVTITHLLKA103 GDQIICMDDV113 YGGTNRYFRQ123 VASEFGLKIS 133 FVDCSKIKLL143 EAAITPETKL153 VWIETPTNPT163 QKVIDIEGCA173 HIVHKHGDII 183 LVVDNTFMSP193 YFQRPLALGA203 DISMYSATKY213 MNGHSDVVMG223 LVSVNCESLH 233 NRLRFLQNSL243 GAVPSPIDCY253 LCNRGLKTLH263 VRMEKHFKNG273 MAVAQFLESN 283 PWVEKVIYPG293 LPSHPQHELV303 KRQCTGCTGM313 VTFYIKGTLQ323 HAEIFLKNLK 333 LFTLAESLGG343 FESLAELPAI353 MTHASVLKND363 RDVLGISDTL373 IRLSVGLEDE 383 EDLLEDLDQA393 LKAAHP
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| Ligand Name: L-methionine | Ligand Info | |||||
| Structure Description | Active conformation for Engineered human cystathionine gamma lyase (E59N, R119L, E339V) to depleting methionine | PDB:5TSU | ||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | Yes | [2] |
| PDB Sequence |
GFLPHFQHFA
19 TQAIHVGQDP29 EQWTSRAVVP39 PISLSTTFKQ49 GGFNYSRSGN65 PTRNCLEKAV 75 AALDGAKYCL85 AFASGLAATV95 TITHLLKAGD105 QIICMDDVYG115 GTNLYFRQVA 125 SEFGLKISFV135 DCSKIKLLEA145 AITPETKLVW155 IETPTNPTQK165 VIDIEGCAHI 175 VHKHGDIILV185 VDNTFMSPYF195 QRPLALGADI205 SMYSATYMNG216 HSDVVMGLVS 226 VNCESLHNRL236 RFLQNSLGAV246 PSPIDCYLCN256 RGLKTLHVRM266 EKHFKNGMAV 276 AQFLESNPWV286 EKVIYPGLPS296 HPQHELVKRQ306 CTGCTGMVTF316 YIKGTLQHAE 326 IFLKNLKLFT336 LAVSLGGFES346 LAELPAIMTH356 ASVKNDRDVL367 GISDTLIRLS 377 VGLEDEEDLL387 EDLDQALKAA397 HPP
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MET or .MET2 or .MET3 or :3MET;style chemicals stick;color identity;select .A:114 or .A:161 or .A:339 or .A:340 or .A:341 or .A:349 or .A:354 or .A:355 or .A:375; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: 2-[({3-Hydroxy-2-Methyl-5-[(Phosphonooxy)methyl]pyridin-4-Yl}methyl)amino]acrylic Acid | Ligand Info | |||||
| Structure Description | Crystal structure of Human Cystathionine gamma lyase with S-3-Carboxpropyl-L-Cysteine | PDB:6NBA | ||||
| Method | X-ray diffraction | Resolution | 2.50 Å | Mutation | No | [3] |
| PDB Sequence |
GFLPHFQHFA
19 TQAIHVGQDP29 EQWTSRAVVP39 PISLSTTFKQ49 GAPGQHSGFE59 YSRSGNPTRN 69 CLEKAVAALD79 GAKYCLAFAS89 GLAATVTITH99 LLKAGDQIIC109 MDDVYGGTNR 119 YFRQVASEFG129 LKISFVDCSK139 IKLLEAAITP149 ETKLVWIETP159 TNPTQKVIDI 169 EGCAHIVHKH179 GDIILVVDNT189 FMSPYFQRPL199 ALGADISMYS209 ATKYMNGHSD 219 VVMGLVSVNC229 ESLHNRLRFL239 QNSLGAVPSP249 IDCYLCNRGL259 KTLHVRMEKH 269 FKNGMAVAQF279 LESNPWVEKV289 IYPGLPSHPQ299 HELVKRQCTG309 CTGMVTFYIK 319 GTLQHAEIFL329 KNLKLFTLAE339 SLGGFESLAE349 LPAIMTHASV359 LKNDRDVLGI 369 SDTLIRLSVG379 LEDEEDLLED389 LDQALKAAH
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .P1T or .P1T2 or .P1T3 or :3P1T;style chemicals stick;color identity;select .A:89 or .A:90 or .A:91 or .A:114 or .A:117 or .A:157 or .A:161 or .A:187 or .A:189 or .A:190 or .A:207 or .A:209 or .A:211 or .A:212 or .A:221 or .A:222 or .A:339 or .A:340 or .A:341 or .A:349 or .A:355 or .A:356 or .A:375; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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SER89
3.702
GLY90
2.643
LEU91
3.176
TYR114
3.413
THR117
4.248
GLU157
3.439
ASN161
3.043
ASP187
2.894
THR189
3.792
PHE190
4.217
MET207
4.474
SER209
2.851
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| Ligand Name: (2S)-2-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]-4-methylsulfanylbutanoic acid | Ligand Info | |||||
| Structure Description | Active conformation for Engineered human cystathionine gamma lyase (E59N, R119L, E339V) to depleting methionine | PDB:5TSU | ||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | Yes | [2] |
| PDB Sequence |
GFLPHFQHFA
19 TQAIHVGQDP29 EQWTSRAVVP39 PISLSTTFKQ49 GSGFNYSRSG64 NPTRNCLEKA 74 VAALDGAKYC84 LAFASGLAAT94 VTITHLLKAG104 DQIICMDDVY114 GGTNLYFRQV 124 ASEFGLKISF134 VDCSKIKLLE144 AAITPETKLV154 WIETPTNPTQ164 KVIDIEGCAH 174 IVHKHGDIIL184 VVDNTFMSPY194 FQRPLALGAD204 ISMYSATKYM214 NGHSDVVMGL 224 VSVNCESLHN234 RLRFLQNSLG244 AVPSPIDCYL254 CNRGLKTLHV264 RMEKHFKNGM 274 AVAQFLESNP284 WVEKVIYPGL294 PSHPQHELVK304 RQCTGCTGMV314 TFYIKGTLQH 324 AEIFLKNLKL334 FTLAVSLGGF344 ESLAELPAIM354 THASVLKNDR364 DVLGISDTLI 374 RLSVGLEDEE384 DLLEDLDQAL394 KAAHPP
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .LPI or .LPI2 or .LPI3 or :3LPI;style chemicals stick;color identity;select .C:89 or .C:90 or .C:91 or .C:92 or .C:114 or .C:117 or .C:157 or .C:161 or .C:187 or .C:189 or .C:190 or .C:207 or .C:209 or .C:211 or .C:212 or .C:221 or .C:222 or .C:339 or .C:340 or .C:341 or .C:354 or .C:355 or .C:356 or .C:375; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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SER89
3.367
GLY90
2.860
LEU91
2.858
ALA92
4.966
TYR114
2.979
THR117
4.337
GLU157
3.575
ASN161
3.045
ASP187
2.836
THR189
3.784
PHE190
4.103
MET207
4.571
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| Ligand Name: N6-((3-Hydroxy-2-methyl-5-((phosphonooxy)methyl)-4-pyridinyl)methylene)-L-lysine | Ligand Info | |||||
| Structure Description | Active conformation for Engineered human cystathionine gamma lyase (E59N, R119L, E339V) to depleting methionine | PDB:5TSU | ||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | Yes | [2] |
| PDB Sequence |
GFLPHFQHFA
19 TQAIHVGQDP29 EQWTSRAVVP39 PISLSTTFKQ49 GGFNYSRSGN65 PTRNCLEKAV 75 AALDGAKYCL85 AFASGLAATV95 TITHLLKAGD105 QIICMDDVYG115 GTNLYFRQVA 125 SEFGLKISFV135 DCSKIKLLEA145 AITPETKLVW155 IETPTNPTQK165 VIDIEGCAHI 175 VHKHGDIILV185 VDNTFMSPYF195 QRPLALGADI205 SMYSATYMNG216 HSDVVMGLVS 226 VNCESLHNRL236 RFLQNSLGAV246 PSPIDCYLCN256 RGLKTLHVRM266 EKHFKNGMAV 276 AQFLESNPWV286 EKVIYPGLPS296 HPQHELVKRQ306 CTGCTGMVTF316 YIKGTLQHAE 326 IFLKNLKLFT336 LAVSLGGFES346 LAELPAIMTH356 ASVKNDRDVL367 GISDTLIRLS 377 VGLEDEEDLL387 EDLDQALKAA397 HPP
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .LLP or .LLP2 or .LLP3 or :3LLP;style chemicals stick;color identity;select .A:89 or .A:90 or .A:91 or .A:92 or .A:114 or .A:117 or .A:157 or .A:161 or .A:187 or .A:189 or .A:190 or .A:207 or .A:209 or .A:210 or .A:211 or .A:213 or .A:214 or .A:215 or .A:216 or .A:217 or .A:221 or .A:222 or .A:340 or .A:341 or .A:342 or .A:343; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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SER89
3.453
GLY90
2.873
LEU91
2.878
ALA92
4.992
TYR114
3.315
THR117
4.507
GLU157
3.336
ASN161
3.080
ASP187
2.724
THR189
3.483
PHE190
4.251
MET207
4.375
SER209
2.891
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S. J Biol Chem. 2009 Jan 30;284(5):3076-3085. | ||||
| REF 2 | Structural Snapshots of an Engineered Cystathionine-Gamma-lyase Reveal the Critical Role of Electrostatic Interactions in the Active Site. Biochemistry. 2017 Feb 14;56(6):876-885. | ||||
| REF 3 | S-3-Carboxypropyl-l-cysteine specifically inhibits cystathionine Gamma-lyase-dependent hydrogen sulfide synthesis. J Biol Chem. 2019 Jul 12;294(28):11011-11022. | ||||
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