6CJA
Crystal structure of Cystathionine beta-lyase from Legionella pneumophila Philadelphia 1 in complex with Alanyl-PLP and Serine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003962 | molecular_function | cystathionine gamma-synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0016829 | molecular_function | lyase activity |
A | 0016846 | molecular_function | carbon-sulfur lyase activity |
A | 0019346 | biological_process | transsulfuration |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0003962 | molecular_function | cystathionine gamma-synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0016829 | molecular_function | lyase activity |
B | 0016846 | molecular_function | carbon-sulfur lyase activity |
B | 0019346 | biological_process | transsulfuration |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0003962 | molecular_function | cystathionine gamma-synthase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0016829 | molecular_function | lyase activity |
C | 0016846 | molecular_function | carbon-sulfur lyase activity |
C | 0019346 | biological_process | transsulfuration |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0003962 | molecular_function | cystathionine gamma-synthase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0016829 | molecular_function | lyase activity |
D | 0016846 | molecular_function | carbon-sulfur lyase activity |
D | 0019346 | biological_process | transsulfuration |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue F0G A 401 |
Chain | Residue |
A | SER76 |
A | SER328 |
A | THR343 |
A | ARG363 |
B | TYR47 |
B | ARG49 |
A | GLY77 |
A | MET78 |
A | TYR101 |
A | ASN149 |
A | ASP174 |
A | SER196 |
A | THR198 |
A | LYS199 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue SER A 402 |
Chain | Residue |
A | TYR101 |
A | ARG106 |
A | GLU327 |
A | MET342 |
A | THR343 |
A | HOH520 |
A | HOH729 |
A | HOH750 |
B | GLU46 |
B | ARG49 |
B | THR50 |
B | ASN229 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | LYS35 |
A | HIS42 |
A | LEU43 |
A | HOH526 |
A | HOH793 |
D | GLY22 |
D | HOH570 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue SER A 404 |
Chain | Residue |
A | GLU46 |
A | ARG49 |
A | THR50 |
A | ASN229 |
B | TYR101 |
B | ARG106 |
B | GLU327 |
B | MET342 |
B | THR343 |
B | HOH520 |
B | HOH772 |
site_id | AC5 |
Number of Residues | 14 |
Details | binding site for residue F0G B 401 |
Chain | Residue |
A | TYR47 |
A | ARG49 |
B | SER76 |
B | GLY77 |
B | MET78 |
B | TYR101 |
B | ASN149 |
B | ASP174 |
B | SER196 |
B | THR198 |
B | LYS199 |
B | SER328 |
B | THR343 |
B | ARG363 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL B 402 |
Chain | Residue |
B | LYS35 |
B | HIS42 |
B | LEU43 |
B | HOH569 |
B | HOH596 |
C | GLY22 |
C | HOH562 |
site_id | AC7 |
Number of Residues | 14 |
Details | binding site for residue F0G C 400 |
Chain | Residue |
C | SER76 |
C | GLY77 |
C | MET78 |
C | TYR101 |
C | ASN149 |
C | ASP174 |
C | SER196 |
C | THR198 |
C | LYS199 |
C | SER328 |
C | THR343 |
C | ARG363 |
D | TYR47 |
D | ARG49 |
site_id | AC8 |
Number of Residues | 11 |
Details | binding site for residue SER C 401 |
Chain | Residue |
C | TYR101 |
C | ARG106 |
C | GLU327 |
C | MET342 |
C | HOH516 |
C | HOH565 |
C | HOH665 |
D | GLU46 |
D | ARG49 |
D | THR50 |
D | ASN229 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue GOL C 402 |
Chain | Residue |
C | GLU311 |
C | ASP312 |
C | ARG315 |
C | HOH563 |
C | HOH585 |
C | HOH601 |
D | LYS273 |
D | ASP312 |
D | HOH584 |
site_id | AD1 |
Number of Residues | 15 |
Details | binding site for residue F0G D 400 |
Chain | Residue |
C | TYR47 |
C | ARG49 |
D | SER76 |
D | GLY77 |
D | MET78 |
D | TYR101 |
D | ASN149 |
D | ASP174 |
D | SER196 |
D | THR198 |
D | LYS199 |
D | SER328 |
D | LEU329 |
D | THR343 |
D | ARG363 |
site_id | AD2 |
Number of Residues | 11 |
Details | binding site for residue SER D 401 |
Chain | Residue |
C | GLU46 |
C | ARG49 |
C | THR50 |
C | ASN229 |
D | TYR101 |
D | ARG106 |
D | GLU327 |
D | MET342 |
D | HOH524 |
D | HOH642 |
D | HOH701 |
Functional Information from PROSITE/UniProt
site_id | PS00868 |
Number of Residues | 15 |
Details | CYS_MET_METAB_PP Cys/Met metabolism enzymes pyridoxal-phosphate attachment site. DIvlhSATKYLnGHS |
Chain | Residue | Details |
A | ASP191-SER205 |