3VPD
LysX from Thermus thermophilus complexed with AMP-PNP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009432 | biological_process | SOS response |
| A | 0016874 | molecular_function | ligase activity |
| A | 0018169 | molecular_function | ribosomal S6-glutamic acid ligase activity |
| A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| A | 0036211 | biological_process | protein modification process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0072590 | molecular_function | N-acetyl-L-aspartate-L-glutamate ligase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009432 | biological_process | SOS response |
| B | 0016874 | molecular_function | ligase activity |
| B | 0018169 | molecular_function | ribosomal S6-glutamic acid ligase activity |
| B | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| B | 0036211 | biological_process | protein modification process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0072590 | molecular_function | N-acetyl-L-aspartate-L-glutamate ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ANP A 301 |
| Chain | Residue |
| A | VAL127 |
| A | ASP178 |
| A | ARG180 |
| A | ARG194 |
| A | TRP199 |
| A | ILE200 |
| A | THR201 |
| A | ASP237 |
| A | PHE239 |
| A | ASN248 |
| A | GLU249 |
| A | LYS129 |
| A | ASN251 |
| A | TRP135 |
| A | GLY136 |
| A | LEU139 |
| A | GLN169 |
| A | GLU170 |
| A | VAL172 |
| A | LYS174 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BUA A 302 |
| Chain | Residue |
| A | THR203 |
| A | PHE256 |
| A | LYS257 |
| A | ASN258 |
| A | SER259 |
| A | HOH608 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CIT A 303 |
| Chain | Residue |
| A | VAL57 |
| A | SER58 |
| A | GLN59 |
| A | SER60 |
| A | GLY133 |
| A | TRP135 |
| A | HOH585 |
| A | HOH597 |
| B | PHE161 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ANP B 301 |
| Chain | Residue |
| B | VAL127 |
| B | LYS129 |
| B | GLN169 |
| B | GLU170 |
| B | TYR171 |
| B | VAL172 |
| B | LYS174 |
| B | ASP178 |
| B | ARG180 |
| B | ARG194 |
| B | PHE239 |
| B | ASN248 |
| B | GLU249 |
| B | HOH426 |
| B | HOH496 |
| B | HOH532 |
| B | HOH575 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BUA B 302 |
| Chain | Residue |
| B | GLU255 |
| B | PHE256 |
| B | LYS257 |
| B | ASN258 |
| B | SER259 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS89 | |
| B | ASN251 | |
| A | ASN202 | |
| A | ASP237 | |
| A | GLU249 | |
| A | ASN251 | |
| B | LYS89 | |
| B | ASN202 | |
| B | ASP237 | |
| B | GLU249 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS129 | |
| A | GLY133 | |
| A | GLN169 | |
| A | ARG194 | |
| B | LYS129 | |
| B | GLY133 | |
| B | GLN169 | |
| B | ARG194 |
