4RLG
The clear crystal structure of pyridoxal-dependent decarboxylase from sphaerobacter thermophilus dsm 20745
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
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 | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
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 | 0019752 | biological_process | carboxylic acid metabolic process |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
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 | 0019752 | biological_process | carboxylic acid metabolic process |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE PMP A 2001 |
Chain | Residue |
A | MSE91 |
A | ALA274 |
A | ASN301 |
A | GLN303 |
A | LLP304 |
A | HOH2148 |
A | HOH2186 |
A | HOH2218 |
B | THR351 |
B | HOH634 |
A | GLY150 |
A | GLY151 |
A | SER152 |
A | ASN155 |
A | HIS190 |
A | GLY245 |
A | THR247 |
A | ASP272 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 2002 |
Chain | Residue |
A | ARG384 |
A | GLY388 |
A | GLN391 |
A | ARG392 |
A | ASP465 |
A | PHE468 |
A | HOH2361 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE K A 2003 |
Chain | Residue |
A | VAL389 |
A | ARG392 |
A | LEU395 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PMP B 501 |
Chain | Residue |
A | THR351 |
B | MSE91 |
B | GLY150 |
B | GLY151 |
B | SER152 |
B | HIS190 |
B | GLY245 |
B | THR247 |
B | ASP272 |
B | ALA274 |
B | ASN301 |
B | GLN303 |
B | LLP304 |
B | HOH601 |
B | HOH680 |
B | HOH893 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 502 |
Chain | Residue |
B | SER115 |
B | GLU117 |
B | MSE118 |
B | HOH754 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 503 |
Chain | Residue |
B | ARG384 |
B | GLU387 |
B | GLY388 |
B | ASP465 |
B | PHE468 |
B | HOH843 |
B | HOH901 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE K B 504 |
Chain | Residue |
B | VAL389 |
B | ARG392 |
B | LEU395 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PMP D 501 |
Chain | Residue |
C | THR351 |
C | HOH611 |
D | MSE91 |
D | GLY150 |
D | GLY151 |
D | SER152 |
D | HIS190 |
D | GLY245 |
D | THR247 |
D | ASP272 |
D | ALA274 |
D | ASN301 |
D | GLN303 |
D | LLP304 |
D | HOH660 |
D | HOH869 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ABU D 502 |
Chain | Residue |
D | SER186 |
D | ALA188 |
D | ALA189 |
D | HIS190 |
D | THR191 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ABU D 503 |
Chain | Residue |
D | ALA189 |
D | HIS190 |
D | THR191 |
D | LEU193 |
D | GLN194 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL D 504 |
Chain | Residue |
D | ARG384 |
D | GLU387 |
D | GLN391 |
D | ASP465 |
D | PHE468 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K D 505 |
Chain | Residue |
D | VAL389 |
D | ARG390 |
D | ARG392 |
D | LEU395 |
site_id | BC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PMP C 501 |
Chain | Residue |
C | GLY245 |
C | THR247 |
C | ASP272 |
C | ALA274 |
C | ASN301 |
C | GLN303 |
C | LLP304 |
C | HOH632 |
C | HOH683 |
C | HOH872 |
D | THR351 |
C | MSE91 |
C | GLY150 |
C | GLY151 |
C | SER152 |
C | ASN155 |
C | HIS190 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 502 |
Chain | Residue |
C | ARG384 |
C | GLY388 |
C | ASP465 |
C | PHE468 |
C | HOH810 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE K C 503 |
Chain | Residue |
C | VAL389 |
C | ARG392 |
C | LEU395 |