2FP4
Crystal structure of pig GTP-specific succinyl-CoA synthetase in complex with GTP
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 | 4 |
Details | BINDING SITE FOR RESIDUE K B 401 |
Chain | Residue |
B | ASN206 |
B | ASP220 |
B | GTP403 |
B | HOH488 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 402 |
Chain | Residue |
B | SER165 |
B | GTP404 |
B | HOH499 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE GTP B 403 |
Chain | Residue |
B | GLY52 |
B | GLY53 |
B | ARG54 |
B | GLY55 |
B | VAL67 |
B | LEU69 |
B | ALA108 |
B | LEU109 |
B | GLU114 |
B | PHE219 |
B | ASP220 |
B | LYS222 |
B | K401 |
B | HOH487 |
B | HOH488 |
B | HOH489 |
B | HOH511 |
B | GLN20 |
B | VAL44 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GTP B 404 |
Chain | Residue |
A | LYS50 |
B | GLY55 |
B | LYS56 |
B | LYS64 |
B | LYS163 |
B | ASP164 |
B | SER165 |
B | GLN168 |
B | ARG169 |
B | GLU172 |
B | MG402 |
B | HOH474 |
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 |
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 |