6ZEK
Crystal structure of mouse CSAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004068 | molecular_function | aspartate 1-decarboxylase activity |
| A | 0004782 | molecular_function | sulfinoalanine decarboxylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019449 | biological_process | L-cysteine catabolic process to hypotaurine |
| A | 0019452 | biological_process | L-cysteine catabolic process to taurine |
| A | 0019530 | biological_process | taurine metabolic process |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042412 | biological_process | taurine biosynthetic process |
| B | 0004068 | molecular_function | aspartate 1-decarboxylase activity |
| B | 0004782 | molecular_function | sulfinoalanine decarboxylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019449 | biological_process | L-cysteine catabolic process to hypotaurine |
| B | 0019452 | biological_process | L-cysteine catabolic process to taurine |
| B | 0019530 | biological_process | taurine metabolic process |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042412 | biological_process | taurine biosynthetic process |
| C | 0004068 | molecular_function | aspartate 1-decarboxylase activity |
| C | 0004782 | molecular_function | sulfinoalanine decarboxylase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019449 | biological_process | L-cysteine catabolic process to hypotaurine |
| C | 0019452 | biological_process | L-cysteine catabolic process to taurine |
| C | 0019530 | biological_process | taurine metabolic process |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042412 | biological_process | taurine biosynthetic process |
| D | 0004068 | molecular_function | aspartate 1-decarboxylase activity |
| D | 0004782 | molecular_function | sulfinoalanine decarboxylase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019449 | biological_process | L-cysteine catabolic process to hypotaurine |
| D | 0019452 | biological_process | L-cysteine catabolic process to taurine |
| D | 0019530 | biological_process | taurine metabolic process |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0042412 | biological_process | taurine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | GLU45 |
| A | LYS47 |
| A | HIS79 |
| A | TYR80 |
| A | HOH627 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CO A 502 |
| Chain | Residue |
| A | HOH767 |
| A | ILE395 |
| A | LYS396 |
| A | ARG398 |
| A | PHE401 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | GLN355 |
| A | ARG359 |
| C | GLN312 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 504 |
| Chain | Residue |
| A | LYS134 |
| A | TRP369 |
| A | GLY374 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | GLN92 |
| A | LEU93 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| B | HIS286 |
| B | HIS288 |
| B | GLU408 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CO B 502 |
| Chain | Residue |
| B | ILE395 |
| B | LYS396 |
| B | ARG398 |
| B | PHE401 |
| B | HOH699 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | ALA386 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 504 |
| Chain | Residue |
| B | GLN355 |
| B | ARG359 |
| D | GLN312 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 505 |
| Chain | Residue |
| B | LYS134 |
| B | GLY374 |
| D | GLN61 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 506 |
| Chain | Residue |
| B | GLN92 |
| B | LEU93 |
| D | HOH733 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 501 |
| Chain | Residue |
| C | LEU138 |
| C | VAL139 |
| C | GLY140 |
| C | ARG287 |
| C | ASP291 |
| C | GLN294 |
| C | HOH695 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 502 |
| Chain | Residue |
| A | HOH603 |
| C | HIS286 |
| C | HIS288 |
| C | GLU408 |
| C | HOH720 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue CO C 503 |
| Chain | Residue |
| C | ILE395 |
| C | LYS396 |
| C | ARG398 |
| C | PHE401 |
| C | HOH766 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 504 |
| Chain | Residue |
| A | GLN312 |
| C | GLN355 |
| C | ARG359 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 505 |
| Chain | Residue |
| A | GLN61 |
| C | LYS134 |
| C | GLY374 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 506 |
| Chain | Residue |
| C | LEU93 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 501 |
| Chain | Residue |
| B | ARG389 |
| D | HIS286 |
| D | HIS288 |
| D | GLU408 |
| D | HOH638 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue CO D 502 |
| Chain | Residue |
| D | ILE395 |
| D | LYS396 |
| D | ARG398 |
| D | PHE401 |
| D | HOH630 |
| D | HOH723 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 503 |
| Chain | Residue |
| B | GLN312 |
| D | GLN355 |
| D | ARG359 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 504 |
| Chain | Residue |
| B | GLN61 |
| D | LYS134 |
| D | TRP369 |
| site_id | AE4 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 505 |
| Chain | Residue |
| D | GLN92 |
| D | LEU93 |
Functional Information from PROSITE/UniProt
| site_id | PS00392 |
| Number of Residues | 22 |
| Details | DDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SVaWnphKLLaAgLQCsaLLlR |
| Chain | Residue | Details |
| A | SER298-ARG319 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
