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 | 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 | 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 | 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 | 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 | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LLP305 | |
B | LLP305 | |
C | LLP305 | |
D | LLP305 |