Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T62193 | Target Info | |||
| Target Name | Aromatic-L-amino-acid decarboxylase (DDC) | ||||
| Synonyms | DOPA decarboxylase; AADC | ||||
| Target Type | Successful Target | ||||
| Gene Name | DDC | ||||
| Biochemical Class | Carbon-carbon lyase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Pyridoxal phosphate | Ligand Info | |||||
| Structure Description | Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the open conformation with LLP and PLP bound to Chain-A and Chain-B respectively | PDB:3RCH | ||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [1] |
| PDB Sequence |
MNASEFRRRG
10 KEMVDYVANY20 MEGIEGRQVY30 PDVEPGYLRP40 LIPAAAPQEP50 DTFEDIINDV 60 EKIIMPGVTH70 WHSPYFFAYF80 PTASSYPAML90 ADMLCGAIGA107 SPACTELETV 117 MMDWLGKMLE127 LPKAFLNEKA137 GEGGGVIQGS147 ASEATLVALL157 AARTKVIHRL 167 QAASPELTQA177 AIMEKLVAYS187 SDQAHSSVER197 AGLIGGVKLK207 AIPSDGNFAM 217 RASALQEALE227 RDKAAGLIPF237 FMVATLGTTT247 CCSFDNLLEV257 GPICNKEDIW 267 LHVDAAYAGS277 AFICPEFRHL287 LNGVEFADSF297 NFNPHKWLLV307 NFDCSAMWVK 317 KRTDLRFRSL360 KMWFVFRMYG370 VKGLQAYIRK380 HVQLSHEFES390 LVRQDPRFEI 400 CVEVILGLVC410 FRLKGSNKVN420 EALLQRINSA430 KKIHLVPCHL440 RDKFVLRFAI 450 CSRTVESAHV460 QRAWEHIKEL470 AADVLRAERE480
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: N6-((3-Hydroxy-2-methyl-5-((phosphonooxy)methyl)-4-pyridinyl)methylene)-L-lysine | Ligand Info | |||||
| Structure Description | Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the open conformation with LLP and PLP bound to Chain-A and Chain-B respectively | PDB:3RCH | ||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [1] |
| PDB Sequence |
MNASEFRRRG
10 KEMVDYVANY20 MEGIEGRQVY30 PDVEPGYLRP40 LIPAAAPQEP50 DTFEDIINDV 60 EKIIMPGVTH70 WHSPYFFAYF80 PTASSYPAML90 ADMLCGAIGC100 ISPACTELET 116 VMMDWLGKML126 ELPKAFLNEK136 AGEGGGVIQG146 SASEATLVAL156 LAARTKVIHR 166 LQAASPELTQ176 AAIMEKLVAY186 SSDQAHSSVE196 RAGLIGGVKL206 KAIPSDGNFA 216 MRASALQEAL226 ERDKAAGLIP236 FFMVATLGTT246 TCCSFDNLLE256 VGPICNKEDI 266 WLHVDAAYAG276 SAFICPEFRH286 LLNGVEFADS296 FNFNPHWLLV307 NFDCSAMWVK 317 KRTDLTGAFR355 RFRSLKMWFV365 FRMYGVKGLQ375 AYIRKHVQLS385 HEFESLVRQD 395 PRFEICVEVI405 LGLVCFRLKG415 SNKVNEALLQ425 RINSAKKIHL435 VPCHLRDKFV 445 LRFAICSRTV455 ESAHVQRAWE465 HIKELAADVL475 RAERE
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TYR79
3.051
PHE80
3.991
PRO81
2.468
THR82
3.654
ALA83
3.401
GLY146
4.747
SER147
3.104
ALA148
2.968
SER149
2.794
HIS192
3.241
SER194
4.163
THR242
3.838
GLY244
3.724
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases. Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20514-9. | ||||
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