Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004775 | molecular_function | succinate-CoA ligase (ADP-forming) activity |
B | 0004776 | molecular_function | succinate-CoA ligase (GDP-forming) activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005525 | molecular_function | GTP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006104 | biological_process | succinyl-CoA metabolic process |
B | 0016874 | molecular_function | ligase activity |
B | 0042709 | cellular_component | succinate-CoA ligase complex |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 307 |
Chain | Residue |
A | ARG255 |
A | ARG256 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 396 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 397 |
Chain | Residue |
A | LYS53 |
B | LYS163 |
B | ASP164 |
B | SER165 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 308 |
Chain | Residue |
A | HOH354 |
B | LYS64 |
A | THR46 |
Functional Information from PROSITE/UniProt
site_id | PS00399 |
Number of Residues | 14 |
Details | SUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GltAppgr...RMGHAG |
Chain | Residue | Details |
A | GLY248-GLY261 | |
site_id | PS01216 |
Number of Residues | 30 |
Details | SUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGTLTyEavhqttqvglGqslcVGIGGD |
Chain | Residue | Details |
A | SER160-ASP189 | |
site_id | PS01217 |
Number of Residues | 26 |
Details | SUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GnIacFvNGAGLAmatcDiIflngGK |
Chain | Residue | Details |
B | GLY264-LYS289 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | NEP259 | |
B | GLY53 | |
B | LEU109 | |
Chain | Residue | Details |
A | THR24 | |
A | LYS50 | |
A | ILE103 | |
Chain | Residue | Details |
A | TYR167 | |
B | GLY328 | |
Chain | Residue | Details |
A | LYS14 | |
B | ASP110 | |
Chain | Residue | Details |
A | LYS17 | |
A | LYS26 | |
B | LYS102 | |
B | LYS163 | |
B | LYS234 | |
B | LYS310 | |
B | LYS349 | |
B | LYS386 | |
Chain | Residue | Details |
A | LYS65 | |
B | LYS301 | |
Chain | Residue | Details |
A | LYS298 | |
Chain | Residue | Details |
B | LYS190 | |
B | LYS254 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1cqj |
Chain | Residue | Details |
A | GLU217 | |
B | GLU204 | |
B | TYR116 | |