1SCU
THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI AT 2.5 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004775 | molecular_function | succinate-CoA ligase (ADP-forming) activity |
| A | 0004776 | molecular_function | succinate-CoA ligase (GDP-forming) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0009361 | cellular_component | succinate-CoA ligase complex (ADP-forming) |
| A | 0016874 | molecular_function | ligase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006104 | biological_process | succinyl-CoA metabolic process |
| B | 0009361 | cellular_component | succinate-CoA ligase complex (ADP-forming) |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042709 | cellular_component | succinate-CoA ligase complex |
| B | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004775 | molecular_function | succinate-CoA ligase (ADP-forming) activity |
| D | 0004776 | molecular_function | succinate-CoA ligase (GDP-forming) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0009361 | cellular_component | succinate-CoA ligase complex (ADP-forming) |
| D | 0016874 | molecular_function | ligase activity |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004775 | molecular_function | succinate-CoA ligase (ADP-forming) activity |
| E | 0004776 | molecular_function | succinate-CoA ligase (GDP-forming) activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0006099 | biological_process | tricarboxylic acid cycle |
| E | 0006104 | biological_process | succinyl-CoA metabolic process |
| E | 0009361 | cellular_component | succinate-CoA ligase complex (ADP-forming) |
| E | 0016874 | molecular_function | ligase activity |
| E | 0042709 | cellular_component | succinate-CoA ligase complex |
| E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE COA A 289 |
| Chain | Residue |
| A | GLY14 |
| A | TYR71 |
| A | VAL72 |
| A | PRO73 |
| A | SER80 |
| A | ILE95 |
| A | THR96 |
| A | GLU97 |
| A | ASN122 |
| A | CYS123 |
| A | PRO124 |
| A | THR16 |
| A | HOH293 |
| A | HOH294 |
| B | ARG161 |
| E | ARG29 |
| E | GLU33 |
| E | SER36 |
| E | LYS66 |
| A | GLY17 |
| A | SER18 |
| A | GLN19 |
| A | VAL38 |
| A | THR39 |
| A | PRO40 |
| A | LYS42 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE COA D 289 |
| Chain | Residue |
| B | GLU33 |
| B | SER36 |
| B | LYS66 |
| D | GLY14 |
| D | THR16 |
| D | GLY17 |
| D | SER18 |
| D | GLN19 |
| D | VAL38 |
| D | PRO40 |
| D | LYS42 |
| D | TYR71 |
| D | VAL72 |
| D | PRO73 |
| D | SER80 |
| D | ILE95 |
| D | THR96 |
| D | GLU97 |
| D | ASN122 |
| D | CYS123 |
| D | HOH298 |
| D | HOH303 |
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. GvtApkgk...RMGHAG |
| Chain | Residue | Details |
| A | GLY235-GLY248 |
| site_id | PS01216 |
| Number of Residues | 30 |
| Details | SUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGTLTyEavkqttdygfGqstcVGIGGD |
| Chain | Residue | Details |
| A | SER151-ASP180 |
| site_id | PS01217 |
| Number of Residues | 26 |
| Details | SUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GnIgcMvNGAGLAmgtmDiVklhgGE |
| Chain | Residue | Details |
| B | GLY257-GLU282 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10625475 |
| Chain | Residue | Details |
| B | LYS46 | |
| E | GLU99 | |
| E | THR102 | |
| E | GLU107 | |
| E | ASN199 | |
| E | ASP213 | |
| B | GLY53 | |
| B | GLU99 | |
| B | THR102 | |
| B | GLU107 | |
| B | ASN199 | |
| B | ASP213 | |
| E | LYS46 | |
| E | GLY53 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00558 |
| Chain | Residue | Details |
| B | ASN264 | |
| B | GLY321 | |
| E | ASN264 | |
| E | GLY321 | |
| D | GLY43 | |
| D | THR96 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01988 |
| Chain | Residue | Details |
| A | GLU159 | |
| D | GLU159 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cqj |
| Chain | Residue | Details |
| B | TYR109 | |
| B | GLU197 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cqj |
| Chain | Residue | Details |
| E | TYR109 | |
| E | GLU197 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cqj |
| Chain | Residue | Details |
| A | GLU208 | |
| A | NEP246 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cqj |
| Chain | Residue | Details |
| D | GLU208 | |
| D | NEP246 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 476 |
| Chain | Residue | Details |
| B | TYR109 | electrostatic stabiliser, steric role |
| B | GLU197 | electrostatic stabiliser, modifies pKa |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 476 |
| Chain | Residue | Details |
| E | TYR109 | electrostatic stabiliser, steric role |
| E | GLU197 | electrostatic stabiliser, modifies pKa |
