6LDO
Crystal structure of cystathionine gamma-lyase from Lactobacillus plantarum complexed with L-serine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| A | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009086 | biological_process | obsolete methionine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016846 | molecular_function | carbon-sulfur lyase activity |
| A | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| B | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009086 | biological_process | obsolete methionine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016846 | molecular_function | carbon-sulfur lyase activity |
| B | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| C | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009086 | biological_process | obsolete methionine biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016846 | molecular_function | carbon-sulfur lyase activity |
| C | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| D | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009086 | biological_process | obsolete methionine biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016846 | molecular_function | carbon-sulfur lyase activity |
| D | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| D | 0019346 | biological_process | transsulfuration |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| E | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009086 | biological_process | obsolete methionine biosynthetic process |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016846 | molecular_function | carbon-sulfur lyase activity |
| E | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| E | 0019346 | biological_process | transsulfuration |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| F | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009086 | biological_process | obsolete methionine biosynthetic process |
| F | 0016829 | molecular_function | lyase activity |
| F | 0016846 | molecular_function | carbon-sulfur lyase activity |
| F | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| F | 0019346 | biological_process | transsulfuration |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue KOU A 501 |
| Chain | Residue |
| A | SER72 |
| A | SER321 |
| A | LEU322 |
| A | THR336 |
| A | ARG356 |
| B | TYR43 |
| B | ARG45 |
| A | GLY73 |
| A | SER74 |
| A | TYR97 |
| A | ASN144 |
| A | ASP169 |
| A | PHE172 |
| A | SER191 |
| A | SER193 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 A 502 |
| Chain | Residue |
| A | LYS2 |
| A | PHE3 |
| A | HOH675 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 503 |
| Chain | Residue |
| A | TYR97 |
| A | ARG102 |
| A | GLU320 |
| B | GLU42 |
| B | ARG45 |
| B | THR46 |
| B | ASN223 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue KOU B 401 |
| Chain | Residue |
| A | TYR43 |
| A | ARG45 |
| B | SER72 |
| B | GLY73 |
| B | SER74 |
| B | TYR97 |
| B | GLU140 |
| B | ASN144 |
| B | ASP169 |
| B | SER191 |
| B | SER193 |
| B | SER321 |
| B | LEU322 |
| B | THR336 |
| B | ARG356 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 402 |
| Chain | Residue |
| B | LYS2 |
| B | GLN6 |
| B | HIS63 |
| B | HOH509 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 403 |
| Chain | Residue |
| B | ARG121 |
| B | HIS148 |
| B | LYS270 |
| B | TYR272 |
| B | HOH505 |
| B | HOH506 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 404 |
| Chain | Residue |
| A | ARG45 |
| A | THR46 |
| A | ASN223 |
| B | TYR97 |
| B | ARG102 |
| B | GLU320 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for residue KOU C 401 |
| Chain | Residue |
| C | SER72 |
| C | GLY73 |
| C | SER74 |
| C | TYR97 |
| C | GLU140 |
| C | ASN144 |
| C | ASP169 |
| C | SER191 |
| C | SER193 |
| C | SER321 |
| C | LEU322 |
| C | THR336 |
| C | ARG356 |
| D | TYR43 |
| D | ARG45 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 C 402 |
| Chain | Residue |
| C | HIS148 |
| C | LYS270 |
| C | HOH568 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 C 403 |
| Chain | Residue |
| C | TYR97 |
| C | ARG102 |
| C | GLU320 |
| D | ARG45 |
| D | THR46 |
| D | ASN223 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 C 404 |
| Chain | Residue |
| C | LYS2 |
| C | PHE3 |
| site_id | AD3 |
| Number of Residues | 14 |
| Details | binding site for residue KOU D 401 |
| Chain | Residue |
| C | TYR43 |
| C | ARG45 |
| D | SER72 |
| D | GLY73 |
| D | SER74 |
| D | TYR97 |
| D | ASN144 |
| D | ASP169 |
| D | SER191 |
| D | SER193 |
| D | SER321 |
| D | LEU322 |
| D | THR336 |
| D | ARG356 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 D 402 |
| Chain | Residue |
| D | LYS2 |
| D | PHE3 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 D 403 |
| Chain | Residue |
| C | THR46 |
| C | ASN223 |
| D | TYR97 |
| D | ARG102 |
| D | GLU320 |
| C | ARG45 |
| site_id | AD6 |
| Number of Residues | 15 |
| Details | binding site for residue KOU E 401 |
| Chain | Residue |
| E | SER72 |
| E | GLY73 |
| E | SER74 |
| E | TYR97 |
| E | GLU140 |
| E | ASN144 |
| E | ASP169 |
| E | SER191 |
| E | SER193 |
| E | SER321 |
| E | LEU322 |
| E | THR336 |
| E | ARG356 |
| F | TYR43 |
| F | ARG45 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 E 402 |
| Chain | Residue |
| E | LYS2 |
| E | PHE3 |
| E | HOH506 |
| E | HOH512 |
| E | HOH546 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 E 403 |
| Chain | Residue |
| E | TYR97 |
| E | ARG102 |
| E | GLU320 |
| F | ARG45 |
| F | THR46 |
| F | ASN223 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 E 404 |
| Chain | Residue |
| E | ARG45 |
| E | THR46 |
| E | ASN223 |
| F | TYR97 |
| F | ARG102 |
| F | GLU320 |
| site_id | AE1 |
| Number of Residues | 16 |
| Details | binding site for residue KOU F 401 |
| Chain | Residue |
| E | TYR43 |
| E | ARG45 |
| F | SER72 |
| F | GLY73 |
| F | SER74 |
| F | TYR97 |
| F | GLU140 |
| F | ASN144 |
| F | ASP169 |
| F | PHE172 |
| F | SER191 |
| F | SER193 |
| F | SER321 |
| F | LEU322 |
| F | THR336 |
| F | ARG356 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 F 402 |
| Chain | Residue |
| F | LYS2 |
| F | PHE3 |
| F | HOH599 |
