4XX0
CoA bound to pig GTP-specific succinyl-CoA synthetase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| B | 0000166 | molecular_function | nucleotide 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 | 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 | 24 |
| Details | binding site for residue COA A 401 |
| Chain | Residue |
| A | GLY22 |
| A | VAL80 |
| A | PRO81 |
| A | PRO82 |
| A | ILE103 |
| A | THR104 |
| A | GLU105 |
| A | ASN131 |
| A | CYS132 |
| A | PRO133 |
| A | HOH502 |
| A | THR24 |
| A | HOH506 |
| A | HOH528 |
| A | HOH537 |
| A | HOH543 |
| A | HOH592 |
| A | GLY25 |
| A | LYS26 |
| A | GLN27 |
| A | THR46 |
| A | PRO48 |
| A | LYS50 |
| A | TYR79 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 402 |
| Chain | Residue |
| A | SER162 |
| A | GLY163 |
| A | THR164 |
| A | HIS259 |
| A | HOH587 |
| B | GLY272 |
| B | ALA273 |
| B | GLY274 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | GLN122 |
| A | GLY123 |
| A | LYS124 |
| A | HOH596 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | ARG255 |
| A | ARG256 |
| B | LYS258 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | HIS55 |
| A | LEU56 |
| A | HOH553 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | LYS116 |
| A | ASN192 |
| A | GLY193 |
| A | ASP195 |
| A | ASP198 |
| A | HOH539 |
| A | HOH578 |
| A | HOH581 |
| A | HOH601 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| A | ARG155 |
| B | THR70 |
| B | LYS71 |
| B | ASP72 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| A | ARG256 |
| B | MET1 |
| B | ASN224 |
| B | PHE225 |
| B | HOH583 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| B | GLY52 |
| B | GLY53 |
| B | ARG54 |
| B | HOH589 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| B | GLY77 |
| B | GLN78 |
| B | LYS81 |
| B | HOH503 |
| B | HOH510 |
| B | HOH513 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 405 |
| Chain | Residue |
| B | LYS163 |
| B | ASP164 |
| B | SER165 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_03222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10873456","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16481318","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26249701","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03222","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27487822","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P53597","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WUM5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WUM5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WUM5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 228 |
| Details | Domain: {"description":"ATP-grasp","evidences":[{"source":"HAMAP-Rule","id":"MF_03221","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16481318","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16481318","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27487822","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for substrate specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_03221","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Z2I8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9Z2I8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z2I8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q96I99","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
