Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7JJ0

GTP-specific succinyl-CoA synthetase complexed with Mg-GMPPCP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
B0003824molecular_functioncatalytic activity
B0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
B0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0006099biological_processtricarboxylic acid cycle
B0006104biological_processsuccinyl-CoA metabolic process
B0016874molecular_functionligase activity
B0042709cellular_componentsuccinate-CoA ligase complex
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
D0003824molecular_functioncatalytic activity
D0004775molecular_functionsuccinate-CoA ligase (ADP-forming) activity
D0004776molecular_functionsuccinate-CoA ligase (GDP-forming) activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005525molecular_functionGTP binding
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0006099biological_processtricarboxylic acid cycle
D0006104biological_processsuccinyl-CoA metabolic process
D0016874molecular_functionligase activity
D0042709cellular_componentsuccinate-CoA ligase complex
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00399
Number of Residues14
DetailsSUCCINYL_COA_LIG_2 ATP-citrate lyase / succinyl-CoA ligases family active site. GltAppgr...RMGHAG
ChainResidueDetails
AGLY248-GLY261

site_idPS01216
Number of Residues30
DetailsSUCCINYL_COA_LIG_1 ATP-citrate lyase / succinyl-CoA ligases family signature 1. SRSGTLTyEavhqttqvglGqslcVGIGGD
ChainResidueDetails
ASER160-ASP189

site_idPS01217
Number of Residues26
DetailsSUCCINYL_COA_LIG_3 ATP-citrate lyase / succinyl-CoA ligases family signature 3. GnIacFvNGAGLAmatcDiIflngGK
ChainResidueDetails
BGLY264-LYS289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:16481318
ChainResidueDetails
BGLN20
BGLY53
BLEU109
DGLN20
DGLY53
DLEU109

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000305|PubMed:16481318
ChainResidueDetails
BASN206
BASP220
DASN206
DASP220
CLYS50
CILE103

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:27487822
ChainResidueDetails
BASN271
BGLY328
DASN271
DGLY328

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_03221
ChainResidueDetails
BGLU42
BASP110
DGLU42
DASP110

site_idSWS_FT_FI5
Number of Residues16
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2I8
ChainResidueDetails
BLYS36
DLYS95
DLYS102
DLYS163
DLYS234
DLYS310
DLYS349
DLYS386
BLYS95
BLYS102
BLYS163
BLYS234
BLYS310
BLYS349
BLYS386
DLYS36

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9Z2I8
ChainResidueDetails
BLYS41
BLYS301
DLYS41
DLYS301

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z2I8
ChainResidueDetails
BSER124
DSER124

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q96I99
ChainResidueDetails
BLYS190
BLYS254
DLYS190
DLYS254

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon