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 |